Relevant bibliographies by topics / Single Molecule Spectroscopy (SMS)

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'Single Molecule Spectroscopy (SMS)'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Single Molecule Spectroscopy (SMS)"

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Thyrhaug, Erling, Stefan Krause, Antonio Perri, Giulio Cerullo, Dario Polli, Tom Vosch, and Jürgen Hauer. "Single-molecule excitation–emission spectroscopy." Proceedings of the National Academy of Sciences 116, no. 10 (February 15, 2019): 4064–69. http://dx.doi.org/10.1073/pnas.1808290116.

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Single-molecule spectroscopy (SMS) provides a detailed view of individual emitter properties and local environments without having to resort to ensemble averaging. While the last several decades have seen substantial refinement of SMS techniques, recording excitation spectra of single emitters still poses a significant challenge. Here we address this problem by demonstrating simultaneous collection of fluorescence emission and excitation spectra using a compact common-path interferometer and broadband excitation, which is implemented as an extension of a standard SMS microscope. We demonstrate the technique by simultaneously collecting room-temperature excitation and emission spectra of individual terrylene diimide molecules and donor–acceptor dyads embedded in polystyrene. We analyze the resulting spectral parameters in terms of optical lineshape theory to obtain detailed information on the interactions of the emitters with their nanoscopic environment. This analysis finally reveals that environmental fluctuations between the donor and acceptor in the dyads are not correlated.
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Karimullin, Kamil, and Andrei Naumov. "Low-temperature dynamics in a dye-doped polymer: correspondence between the data obtained by photon echo and single molecule spectroscopy." EPJ Web of Conferences 190 (2018): 04008. http://dx.doi.org/10.1051/epjconf/201819004008.

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Low temperature dynamics (tunneling and vibrational relaxation) in doped polyisobutylene film has been reinvestigated using 2-pulse incoherent photon echo (2IPE) and compared with single-molecule spectroscopy (SMS) data. It has been shown that in a very wide range of low temperatures the 2IPE gives optical dephasing times which correspond to the narrowest zero-phonon lines of single dye molecules.
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Li, Chao-Yu, Sai Duan, Jun Yi, Chen Wang, Petar M. Radjenovic, Zhong-Qun Tian, and Jian-Feng Li. "Real-time detection of single-molecule reaction by plasmon-enhanced spectroscopy." Science Advances 6, no. 24 (June 2020): eaba6012. http://dx.doi.org/10.1126/sciadv.aba6012.

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Determining structural transformations of single molecules (SMs) is an important fundamental scientific endeavor. Optical spectroscopies are the dominant tools used to unravel the physical and chemical features of individual molecules and have substantially contributed to surface science and biotechnology. In particular, Raman spectroscopy can identify reaction intermediates and reveal underlying reaction mechanisms; however, SM Raman experiments are subject to intrinsically weak signal intensities and considerable signal attenuation within the spectral dispersion systems of the spectrometer. Here, to monitor the structural transformation of an SM on the millisecond time scale, a plasmonic nanocavity substrate has been used to enable Raman vibrational and fluorescence spectral signals to be simultaneously collected and correlated, which thus allows a detection of photo-induced bond cleavage between the xanthene and phenyl group of a single rhodamine B isothiocyanate molecule in real time. This technique provides a novel method for investigating light-matter interactions and chemical reactions at the SM level.
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Malý, Pavel, J. Michael Gruber, Richard J. Cogdell, Tomáš Mančal, and Rienk van Grondelle. "Ultrafast energy relaxation in single light-harvesting complexes." Proceedings of the National Academy of Sciences 113, no. 11 (February 22, 2016): 2934–39. http://dx.doi.org/10.1073/pnas.1522265113.

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Energy relaxation in light-harvesting complexes has been extensively studied by various ultrafast spectroscopic techniques, the fastest processes being in the sub–100-fs range. At the same time, much slower dynamics have been observed in individual complexes by single-molecule fluorescence spectroscopy (SMS). In this work, we use a pump–probe-type SMS technique to observe the ultrafast energy relaxation in single light-harvesting complexes LH2 of purple bacteria. After excitation at 800 nm, the measured relaxation time distribution of multiple complexes has a peak at 95 fs and is asymmetric, with a tail at slower relaxation times. When tuning the excitation wavelength, the distribution changes in both its shape and position. The observed behavior agrees with what is to be expected from the LH2 excited states structure. As we show by a Redfield theory calculation of the relaxation times, the distribution shape corresponds to the expected effect of Gaussian disorder of the pigment transition energies. By repeatedly measuring few individual complexes for minutes, we find that complexes sample the relaxation time distribution on a timescale of seconds. Furthermore, by comparing the distribution from a single long-lived complex with the whole ensemble, we demonstrate that, regarding the relaxation times, the ensemble can be considered ergodic. Our findings thus agree with the commonly used notion of an ensemble of identical LH2 complexes experiencing slow random fluctuations.
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Kollmann, Heiko, Martin Esmann, Julia Witt, Aleksandra Markovic, Vladimir Smirnov, Gunther Wittstock, Martin Silies, and Christoph Lienau. "Fourier-transform spatial modulation spectroscopy of single gold nanorods." Nanophotonics 7, no. 4 (March 28, 2018): 715–26. http://dx.doi.org/10.1515/nanoph-2017-0096.

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AbstractSensing the scattered fields of single metallic nanostructures is a crucial step towards the applications of isolated plasmonic antennas, such as for the sensing of single molecules or nanoparticles. In the past, both near- and far-field spectroscopy methods have been applied to monitor single plasmonic resonances. So far, however, these spectral-domain techniques do not yet provide the femtosecond time resolution that is needed to probe the dynamics of plasmonic fields in the time domain. Here, we introduce a time-domain technique that combines broadband Fourier-transform spectroscopy and spatial modulation spectroscopy (FT-SMS) to quantitatively measure the extinction spectra of the isolated gold nanorods with a nominal footprint of 41×10 nm2. Using a phase-stable pulse pair for excitation, the technique is capable of rejecting off-resonant stray fields and providing absolute measurements of the extinction cross section. Our results indicate that the method is well suited for measuring the optical response of strongly coupled hybrid systems with high signal-to-noise ratio. It may form the basis for new approaches towards time-domain spectroscopy of single nanoantennas with few-cycle time resolution.
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Torres, Rubén, Begoña Carrasco, and Juan C. Alonso. "Bacillus subtilis RadA/Sms-Mediated Nascent Lagging-Strand Unwinding at Stalled or Reversed Forks Is a Two-Step Process: RadA/Sms Assists RecA Nucleation, and RecA Loads RadA/Sms." International Journal of Molecular Sciences 24, no. 5 (February 25, 2023): 4536. http://dx.doi.org/10.3390/ijms24054536.

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Replication fork rescue requires Bacillus subtilis RecA, its negative (SsbA) and positive (RecO) mediators, and fork-processing (RadA/Sms). To understand how they work to promote fork remodeling, reconstituted branched replication intermediates were used. We show that RadA/Sms (or its variant, RadA/Sms C13A) binds to the 5′-tail of a reversed fork with longer nascent lagging-strand and unwinds it in the 5′→3′ direction, but RecA and its mediators limit unwinding. RadA/Sms cannot unwind a reversed fork with a longer nascent leading-strand, or a gapped stalled fork, but RecA interacts with and activates unwinding. Here, the molecular mechanism by which RadA/Sms, in concert with RecA, in a two-step reaction, unwinds the nascent lagging-strand of reversed or stalled forks is unveiled. First, RadA/Sms, as a mediator, contributes to SsbA displacement from the forks and nucleates RecA onto single-stranded DNA. Then, RecA, as a loader, interacts with and recruits RadA/Sms onto the nascent lagging strand of these DNA substrates to unwind them. Within this process, RecA limits RadA/Sms self-assembly to control fork processing, and RadA/Sms prevents RecA from provoking unnecessary recombination.
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Tricase, Angelo, Anna Imbriano, Nicoletta Ditaranto, Eleonora Macchia, Rosaria Anna Picca, Davide Blasi, Luisa Torsi, and Paolo Bollella. "Electrochemical and X-ray Photoelectron Spectroscopy Surface Characterization of Interchain-Driven Self-Assembled Monolayer (SAM) Reorganization." Nanomaterials 12, no. 5 (March 4, 2022): 867. http://dx.doi.org/10.3390/nano12050867.

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Herein, we report a combined strategy encompassing electrochemical and X-ray photoelectron spectroscopy (XPS) experiments to investigate self-assembled monolayer (SAM) conformational reorganization onto an electrode surface due to the application of an electrical field. In particular, 3-mercaptopriopionic acid SAM (3MPA SAM) modified gold electrodes are activated with a 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysulfosuccinimide (NHSS) (EDC-NHSS) mixture by shortening the activation time, from 2 h to 15/20 min, labelled as Protocol-A, -B and -C, respectively. This step, later followed by a deactivation process with ethanolamine (EA), plays a key role in the reaction yields (formation of N-(2-hydroxyethyl)-3-mercaptopropanamide, NMPA) but also in the conformational rearrangement observed during the application of the electrical field. This study aims at explaining the high performance (i.e., single-molecule detection at a large electrode interface) of bioelectronic devices, where the 3MPA-based SAM structure is pivotal in achieving extremely high sensing performance levels due to its interchain interaction. Cyclic voltammetry (CV) experiments performed in K4Fe(CN)6:K3Fe(CN)6 for 3MPA SAMs that are activated/deactivated show similar trends of anodic peak current (IA) over time, mainly related to the presence of interchain hydrogen bonds, driving the conformational rearrangements (tightening of SAMs structure) while applying an electrical field. In addition, XPS analysis allows correlation of the deactivation yield with electrochemical data (conformational rearrangements), identifying the best protocol in terms of high reaction yield, mainly related to the shorter reaction time, and not triggering any side reactions. Finally, Protocol-C’s SAM surface coverage, determined by CV in H2SO4 and differential pulse voltammetry (DPV) in NaOH, was 1.29 * 1013 molecules cm−2, being similar to the bioreceptor surface coverage in single-molecule detection at a large electrode interface.
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Kilby, P. M., W. U. Primrose, and G. C. K. Roberts. "Changes in the structure of bovine phospholipase A2 upon micelle binding." Biochemical Journal 305, no. 3 (February 1, 1995): 935–44. http://dx.doi.org/10.1042/bj3050935.

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Phospholipase A2 (PLA2) is a calcium-dependent enzyme which hydrolyses the 2-acyl ester bond of phospholipids. The extracellular PLA2s are activated by as much as 10000-fold on binding to micelles or vesicles of substrate, possibly due to a conformational change induced in the enzyme. We have studied the complex of bovine pancreatic PLA2 with micelles of SDS by ultracentrifugation, equilibrium dialysis, microcalorimetry, fluorescence and n.m.r. spectroscopy. Ultracentrifugation and equilibrium dialysis measurements showed that on average 1.28 (+/- 0.17) PLA2 molecules and 26.4 (+/- 3.1) SDS molecules are involved in the complex and that there is a rapid equilibrium between micellar species containing one or more enzyme monomers. The estimated heat of formation of the complex, measured calorimetrically as the heat released when PLA2 was injected into excess 10 mM SDS, was 162.3 +/- 1.5) kJ/mol [38.8 (+/- 0.35) kcal/mol] of PLA2 added. The fluorescence of the single tryptophan at position 3 in the N-terminal helix of the protein increases when PLA2 binds to SDS micelles, indicating that this part of the protein is in a more hydrophobic environment in the complex. The structural changes in PLA2 on addition of [2H25]SDS were monitored using n.m.r. spectroscopy. The overall structure of the protein is unchanged, but changes in nuclear Overhauser effects (NOEs) were observed for residues in the N-terminal helix, at the active site region and in a lysine-rich region near the C-terminus. The NOE changes at the N-terminus indicate that this portion of the protein molecule adopts a more ordered, helical conformation when bound to a micelle. We suggest that these conformational changes could be the mechanism by which the enzyme becomes activated in the presence of aggregated substrate.
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Polikovskiy, Trofim, Vladislav Korshunov, Mikhail Metlin, Viktoria Gontcharenko, Darya Metlina, Nikolay Datskevich, Mikhail Kiskin, Yury Belousov, Alisia Tsorieva, and Ilya Taydakov. "Influence of Ligand Environment Stoichiometry on NIR-Luminescence Efficiency of Sm3+, Pr3+ and Nd3+ Ions Coordination Compounds." Molecules 28, no. 15 (August 5, 2023): 5892. http://dx.doi.org/10.3390/molecules28155892.

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Six new complexes of the ligand HQcy (-4-(cyclohexanecarbonyl)-5-methyl-2-phenyl-2,4-dihydro-3H-pyrazol-3-one) and Ln3+ ions with emission in the near-infrared (Nd3+) or visible and near-infrared (Sm3+, Pr3+) spectral regions were synthesized and characterized using various methods, including single crystal X-ray diffraction. The study demonstrated that both tris complexes [LnQcy3(H2O)(EtOH)] and tetrakis-acids [H3O][LnQcy4] can be synthesized by varying the synthetic conditions. The photochemical properties of the complexes were investigated experimentally and theoretically using various molecular spectroscopy techniques and Judd–Ofelt theory. The objective was to quantitatively and qualitatively disclose the influence of complex stoichiometry on its luminescence properties. The study showed that the addition of an extra ligand molecule (in the tetrakis species) increased molar extinction by up to 2 times, affected the shape of photoluminescence spectra, especially of the Pr3+ complex, and increased the quantum yield of the Sm3+ complex by up to 2 times. The results obtained from this study provide insights into the luminescent properties of lanthanide coordination compounds, which are crucial for the design and development of novel photonic materials with tailored photophysical properties.
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Palacios, Rodrigo E., Fu-Ren F. Fan, Allen J. Bard, and Paul F. Barbara. "Single-Molecule Spectroelectrochemistry (SMS-EC)." Journal of the American Chemical Society 128, no. 28 (July 2006): 9028–29. http://dx.doi.org/10.1021/ja062848e.

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Dissertations / Theses on the topic "Single Molecule Spectroscopy (SMS)"

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Devaux, Floriane. "Synthesis and AFM-based single-molecule force spectroscopy of helical aromatic oligoamide foldamers." Thesis, Bordeaux, 2018. http://www.theses.fr/2018BORD0346.

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Les foldamères sont des architectures moléculaires synthétiques repliées, inspirées par les structures et les fonctions des biopolymères naturels. Le repliement est un processus sélectionné par la nature pour contrôler la conformation de sa machinerie moléculaire afin de réaliser des tâches chimiques ou mécaniques. Durant les dix dernières années de recherche sur les foldamères, des oligomères synthétiques, capables d'adopter des conformations repliées bien définies et prévisibles, comme des hélices, ont été proposés. Les progrès récents ont montré que la synthèse chimique par étapes et le design moléculaire basé sur un squelette oligoamide aromatique permettaient de produire des architectures moléculaires repliées de manière hélicoïdale. La forme du squelette et sa rigidité, des préférences conformationnelles locales, des interactions spécifiques entre monomères éloignés dans une séquence, ainsi que l'action de paramètres externes comme le solvant, ou la présence d'ions peuvent être combinés pour induire une tendance au repliement. Ces architectures sont remarquables car elles peuvent donner lieu à des motifs de repliement qui n'ont pas d'équivalent dans les structures des biopolymères naturels. Par exemple, des hélices dont le diamètre varie le long de la séquence, ou des hélices possédant un centre d'inversion du pas, des hélices en chevrons,... ont été rapportées. Alors que les structures de ces molécules hélicoïdales ont été abondamment caractérisées à l'état solide par cristallographie des rayons X, leur comportement en solution, et surtout le comportement dynamique, est très peu connu. Leurs propriétés mécano-chimiques sont quant à elles inconnues à ce jour. L'objectif du projet est de synthétiser différentes molécules synthétiques hélicoïdales de type oligoamide aromatique et d'obtenir une description détaillée de leur conformation dynamique en solution, ainsi que de leurs propriétés mécano-chimiques, par spectroscopie de force sur molécule unique basée sur l'AFM
Foldamers are artificial folded molecular architectures inspired by the structures and functions of natural biopolymers. Folding is the process selected by nature to control the conformation of its molecular machinery to carry out chemical functions and mechanical tasks, such as en-zyme catalysis, duplication in nucleic acids, force generation,... During the last decade of research on foldamers, synthetic oligomers able to adopt well- defined and predictable folded conformations, such as helices, have been proposed. Recent progress has shown that stepwise chemical synthesis and molecular design based on aromatic oligoamide backbones enable to produce large helically folded molecular architectures. The shape and stiffness of the backbone, local conformational preferences, specific interactions between distant monomers in sequences, as well as the action of external parameters such as the solvent or the presence of ions, can be combine to induce folding tendency. A remarkable aspect of these architectures is that they can give rise to folded patterns that have no in natural counterparts biopolymer structures. For instance, helices whose diameter varies along the se-quence, helices possessing a handedness inversion centre, herringbone helices have been reported. While the structures of these helical molecules have been well characterized in the solid state by X-ray crystallography, much less is known about their dynamic behavior in solution. Their mechanochemical properties are unknown. The objective of the project is to synthesize various helical nanorchitectures based on an oli-goamide aromatic backbone and to obtain a detailed picture of their dynamical conformation in solution, as well as, their mechanochemical properties, by AFM-based single molecule force spectroscopy
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Kirstein, Johanna, Christophe Jung, Christian Hellriegel, and Christoph Bräuchle. "Single molecule spectroscopy." Universitätsbibliothek Leipzig, 2016. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-196553.

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Maity, Sourav. "Single Molecule Force Spectroscopy of CNGA1." Doctoral thesis, SISSA, 2014. http://hdl.handle.net/20.500.11767/3873.

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Single molecule force spectroscopy (SMFS) is known to be one of the most powerful tool to investigate the relation between structure and function in molecules and proteins. The possibility to work in aqueous conditions at a single molecular level opens up an extraordinary perspective to investigate rare events at a molecular level of biological systems. Over the past years Atomic Force Microscopy (AFM) based on SMFS has provided us information, that is either difficult or impossible to get from any other method. In spite of its advancements, SMFS has not been applied to many molecules of biological relevance for several reasons, such as problems with the biological samples, data analysis and other technical issues. Indeed, the development and improvement of SMFS is becoming is very important to study biological molecules and proteins in their natural environment.
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Iordanov, Iordan. "Structure and dynamics of the outer membrane protein A from Klebsiella pneumoniae : a joint NMR–SMFS–proteolysis and MS approach." Toulouse 3, 2012. http://thesesups.ups-tlse.fr/1602/.

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"KpOmpA est une protéine de la membrane externe de K. Pneumoniae. Elle fait partie de la famille des "outer membrane protein A", OmpA. KpOmpA est une protéine constituée de deux domaines: un domaine transmembranaire structuré en tonneau ß et une partie soluble, périplasmique. Le domaine transmembranaire de KpOmpA présente une homologie importante avec celle d'OmpA d'E. Coli dont la structure a été déterminée par cristallographie aux rayons X et spectroscopie RMN. OmpA d'E. Coli est responsable lors de la formation de biofilm. Elle a un rôle d'adhésine et d'invasine. Elle est la cible préférentielle du système immunitaire et est le récepteur de bactériophages. Il est admis que la plupart de ces fonctions sont dues aux boucles extracellulaires de ces protéines. Les différences majeures entre les protéines KpOmpA et OmpA d'E. Coli concernent les boucles extracellulaires de longueur plus importante dans le cas de KpOmpA. Elles jouent un rôle important au cours de l'activation des macrophages et des cellules dendritiques par la voie des récepteurs TLR2. Les boucles extracellulaires jouent un rôle essentiel au cours de l'activation du système immunitaire. Mieux définir la structure et la dynamique de ces boucles est d'une importance essentielle afin de mieux appréhender la fonctionnalité des boucles extracellulaires de KpOmpA. Les informations structurales connues actuellement (structure RMN déterminée dans le groupe IPBS RMN en 2009) ont été obtenus jusqu'à présent avec des échantillons de protéines recombinantes purifiées et repliées dans des micelles de détergent. Dans le présent travail, nous avons d'abord établi un protocole de reconstitution de la protéine dans une membrane phospholipidique et caractérisé nos échantillons par microscopie électronique. Des expériences de spectroscopie de force atomique sur molécule unique ont été réalisées pour caractériser le repliement de la protéine dans son environnement membranaire. Ces expériences suggèrent un nouveau rôle de KpOmpA au sein même de la membrane (collaboration D. Müller, ETH Zürich). Le domaine soluble périplasmique de la protéine a été exprimé indépendamment du domaine membranaire. Les premières expériences HSQC réalisées montrent une structuration de ce domaine. La structure de ce domaine par spectroscopie RMN est en cours de réalisation. Le comportement dynamique des boucles extracellulaires du domaine membranaire KpOmpA reconstitué dans des liposomes a été étudié par spectroscopie RMN à l'angle magique (MAS) et notamment par mesure des temps de relaxation. Nous avons montré que la dynamique intrinsèque de la protéine est indépendante de l'environnement (membrane vs micelle). Des expériences de protéolyse ménagée suivie par spectrométrie de masse (MALDI-TOF) ont été comparées avec les informations RMN afin d'évaluer plus précisément les niveaux de mobilité des différentes boucles extracellulaires. La préservation au cours de l'évolution des boucles extracellulaires semble lier à leur dynamique, ce qui suggère l'importance de ces boucles extracellulaires, en termes de séquence, longueur mais aussi de dynamique lors de la réponse immunitaire. "
KpOmpA is a two-domain membrane protein from Klebsiella pneumoniae belonging to the outer membrane protein A (OmpA) family. It is composed of a transmembrane ß-barrel with 8 ß-strands and a C-terminal, soluble periplasmic domain. The transmembrane domain presents a significant homology with E. Coli OmpA whose three dimensional structure has been determined by X-ray crystallography and by NMR. The E. Coli homologue can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages. It is assumed that most of these functions involve the four protein loops that emanate from the protein to the exterior of the cell. The difference between KpOmpA and E. Coli OmpA is mostly concentrated in these extracellular loops which are larger in the case of KpOmpA. KpOmpA was shown to activate macrophages and dendritic cells through the TLR2 dependent pathway, and these larger loops are supposed to play a specific role in the interactions with the immune system. Thus the structure and dynamics of these loops is of prime functional significance. The currently available information in this regard, including the NMR structure determined in the IPBS NMR group in 2009, have been obtained so far with recombinant protein samples purified and refolded in detergent micelles. In the present work we first established a reconstitution protocol that allowed the incorporation of the membrane protein in the more native environment of the lipid bilayer and characterised our samples by electron microscopy. SMFS experiments were used to probe the reconstituted KpOmpA unfolding-refolding pathways, exploring the folding mechanisms for ß-barrel proteins and suggesting a novel role for OmpA in the bacterial membrane (in collaboration with the group of D. Müller, ETH Zürich). The C-terminal periplasmic domain of KpOmpA was expressed and purified as a separate product and the feasibility of its structure elucidation by NMR was demonstrated by obtaining a high quality HSQC spectrum. The dynamic behaviour of the extracellular portion of the KpOmpA membrane domain reconstituted in liposomes has been investigated by solid state MAS NMR relaxation experiments. We confirmed that the previously observed gradient of dynamic along the molecule axis is an intrinsic property of the protein. Limited proteolysis and MALDI-TOF experiments were coupled with the NMR information in order to assess more precisely the different mobility levels in the loops. Evolutional preservation of the different loops regions is related to their observed flexibility, pointing towards immunologically important, variable, dynamic and accessible loops sections
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Howard, John Brooks. "Double point contact single molecule absorption spectroscopy." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/31648.

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Thesis (Ph.D)--Physics, Georgia Institute of Technology, 2010.
Committee Chair: Marchenkov, Alexei; Committee Member: Davidovic, Dragomir; Committee Member: Gole, James; Committee Member: Hunt, William; Committee Member: Reido, Elisa. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Gryte, Kristofer. "Analysis methods for single molecule fluorescence spectroscopy." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:148969c6-78aa-49c2-8f0e-2d5e5018fd98.

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This thesis describes signal analysis methods for single-molecule fluorescence data. The primary factor motivating method development is the need to distinguish single-molecule FRET fluctuations due to conformational dynamics from fluctuations due to distance-independent FRET changes. Single-molecule Förster resonance energy transfer (FRET) promises a distinct advantage compared to alternative biochemical methods in its potential to relate biomolecular structure to function. Standard measurements assume that the mean transfer efficiency between two fluorescent probes, a donor and an acceptor, corresponds to the mean donor-acceptor distance, thus providing structural information. Accordingly, measurement analysis assumes that mean transfer efficiency fluctuations entail mean donor-acceptor distance fluctuations. Detecting such fluctuations is important in resolving molecular dynamics, as molecular function often necessitates structural changes. A problem arises, however, in that factors other than donor-acceptor distance changes may induce mean transfer efficiency fluctuations. We refer to these factors as distance-independent FRET changes. We present analysis methods to detect distance-independent photophysical dynamics and to determine their correlation with distance-dependent FRET dynamics. First, we review a theory of photon statistics and show how we can use the theory to detect FRET fluctuations. Second, we extend the theory to alternating laser excitation (ALEx) measurements and demonstrate how fluorophore stoichiometry, a measure of fluorophore brightness, reports on distance-independent photophysical dynamics. Next, we provide a measure to determine the extent to which stoichiometry fluctuations account for FRET dynamics. Finally, we use a framework similar to the preceding along with recent advances in the theory of total internal reflection fluorescence (TIRF) microscopy FRET measurements to detect TIRF FRET fluctuations which occur on a timescale faster than the measurement temporal resolution. We validate our methods with simulations and demonstrate their utility in delineating RNA polymerase open complex conformational dynamics.
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Radiom, Milad. "Correlation Force Spectroscopy for Single Molecule Measurements." Diss., Virginia Tech, 2014. http://hdl.handle.net/10919/49677.

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This thesis addresses development of a new force spectroscopy tool, correlation force spectroscopy (CFS), for the measurement of the mechanical properties of very small volumes of material (molecular to µm³) at kHz-MHz time-scales. CFS is based on atomic force microscopy (AFM) and the principles of CFS resemble those of dual-trap optical tweezers. CFS consists of two closely-spaced micro-cantilevers that undergo thermal fluctuations. Measurement of the correlation in thermal fluctuations of the two cantilevers can be used to determine the mechanical properties of the soft matter, e.g. a polymeric molecule, that connects the gap between the two cantilevers. Modeling of the correlations yields the effective stiffness and damping of the molecule. The resolution in stiffness is limited by the stiffness of the cantilever and the frequency by the natural frequency of the cantilevers, but, importantly, the damping resolution is not limited by the damping of the cantilever, which has enabled high-resolution measurements of the internal friction of a polymer. The concept of CFS was originally presented by Roukes' group in Caltech [Arlett et al., Lecture Notes in Physics, 2007]; I developed the first practical versions of CFS for experimentation, and have used it in two applications (1) microrheology of Newtonian fluids and (2) single molecule force spectroscopy. To understand the correlation in thermal fluctuations of two cantilevers I initially validated the theoretical approach for analyzing correlation in terms of deterministic model using the fluctuation-dissipation theorem [Paul and Cross, PRL, 2004]. I have shown that the main advantages of such correlation measurements are a large improvement in the ability to resolve stiffness and damping. Use of CFS as a rheometer was validated by comparison between experimental data and finite element modeling of the deterministic vibrations of the cantilevers using the known viscosity and density of fluids. Work in this thesis shows that the data can also be accurately fitted using a simple harmonic oscillator model, which can be used for rapid rheometric measurements, after calibration. The mechanical properties of biomolecules such as dextran and single stranded DNA (ssDNA) are also described. CFS measurements of single molecule properties of ssDNA reveal the internal friction of the molecule in solution.
Ph. D.
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Iljina, Marija. "Aggregation of alpha-synuclein using single-molecule spectroscopy." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/263216.

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The aggregation of alpha-synuclein (αS) protein from soluble monomer into solid amyloid fibrils in the brain is associated with a range of devastating neurodegenerative disorders such as Parkinson’s disease. Soluble oligomers formed during the aggregation process are highly neurotoxic and are thought to play a key role in the onset and spreading of disease. Despite their importance, these species are difficult to study by conventional experimental approaches owing to their transient nature, heterogeneity, low abundance and a remarkable sensitivity of the oligomerisation process to the chosen experimental conditions. In this thesis, well-established single-molecule techniques have been utilised to study the aggregation and oligomerisation of αS in solution.
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CORTI, ROBERTA. "Single molecule force spectroscopy of proteins and DNA." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2020. http://hdl.handle.net/10281/273770.

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Negli ultimi decenni, lo sviluppo di nuove tecniche di singola molecola ha creato le basi per nuovi paradigmi nel campo della biofisica. In particolare, la nanomanipolazione di singole biomacromolecole ha permesso la caratterizzazione meccanica di proteine e DNA, cercando di evidenziare la relazione fondamentale tra struttura e funzione biologica. Nel corso degli anni sono stati sviluppati diversi metodi di nanomanipolazione: tra questi, il Microscopio a Forza Atomica (AFM), il Magnetic Tweezers (MT) e il Flow-Stretching (F-S) accoppiato a fluorescenza. Queste tre tecniche sono state utilizzate per la caratterizzazione di singole biomacromolecole con tecniche di spettroscopia di forza a livello di singola molecola (SMFS) in quattro diversi progetti. In questa Tesi mi sono occupata principalmente di caratterizzare strutturalmente diverse proteine e correlarne la conformazione alla funzione biologica. In questa ottica, sono state studiate le diverse conformazioni strutturali di una proteina intrinsecamente disordinata (IDP) coinvolta nella malattia del Parkison’s (PD), chiamata alfa-synucleina (AS) e il riarrangiamento strutturale di una proteina coinvolta nel mantenimento strutturale cromosomico, la condensina, durante la condensazione di singoli filamenti di DNA. Inoltre, è stata studiata la struttura di un DNA-analogo sia caratterizzandone la stabilità termica sia attraverso studi di nanomeccanica in SMFS. Infine, è stata descritta una implementazione tecnica di un apparato di F-S accoppiato con illuminazione TIRF, per ottenere una rapida sostituzione di soluzioni durante esperimenti di microfluidica, ottenendo un setup particolarmente indicato per studi di interazione tra DNA e proteine. Durante lo studio della proteina AS in SMFS, il problema della mancanza di una struttura secondaria ben definita è stato risolto con l’impego di una singola poliproteina, contenente un modulo di AS umana. Sono state caratterizzati tre diversi stati conformazionali per AS, da uno stato totalmente destrutturato a una conformazione altamente strutturata. I riarrangiamenti conformazionali di AS sono stati studiati anche in presenza di gallato epigallocatechina (EGCG) e dopamina (DA). Una particolare attenzione è stata quindi riservata al confronto tra i risultati ottenuti da tecniche di SMFS e quelli precedentemente ricavati da analisi di spettroscopia di massa. La proteina AS è stata caratterizzata anche in presenza di tre diverse mutazioni puntuali legate al PD (A30P, A53T e E83A). Nel secondo progetto, un analogo del DNA (DAP) è stato caratterizzato sia con metodi di stabilità termica che di nanomeccanica, studiando il comportamento del DAP-DNA in presenza di forze esterne. L’estensione e la rigidità delle due molecole di DNA (DAP e WT) sono state caratterizzate a basse forze (AFM e MT) e alte forze (MT), dove è stata descritta la transizione di overstretching. Nel terzo progetto è stato studiato l’effetto della condensina sulla condensazione di singoli filamenti di DNA. In particolare, è stato effettuato uno studio di singola molecola per seguire, in tempo reale, la riduzione di estensione di DNA in presenza di condensina e ATP. Considerato che la maggior parte delle curve sono caratterizzate da improvvisi e ben evidenti salti durante la condensazione, sono stati sviluppati e validati due diversi algoritmi per l’identificazione automatica dei gradini. Infine, diverse celle fluidiche sono state testate nell’apparato di F-S, nell’ottica di studi di interazione tra proteine e DNA. Queste celle sono state caratterizzate sia in termini di rapidità di scambio di flussi laminari che di forza capaci di generare sul campione. Sono stati infine visualizzate singole molecole di DNA fluorescenti in presenza di flussi di diversa portata.
In the last few decades, the constant development of novel single molecule techniques has created the basis for a new paradigm in the field of biophysics. Among all, the nanomanipulation of individual biomolecules revealed new insights into the mechanics of biological molecules, in particular proteins and DNA, improving the understanding of the fundamental relation between structural properties and biological functions. Therefore, several single-molecule nanomanipulation methods have been developed, including Atomic Force Microscopy (AFM), Magnetic Tweezers (MT) and Flow Stretching (F-S) coupled with fluorescence. All these technique were employed in this Thesis for the characterisation of biological macromolecules by single molecule force spectroscopy (SMFS). In this Thesis I focus mainly on several aspects of a few different proteins trying to depict a frame in which the strong link between proteins function and their structure can be clarified. With this aim, I study the conformational states of an intrinsically disordered protein (IDP) involved in Parkinson's Disease, the a-synuclein (AS) and the structural change driving the DNA compaction mediated by structural maintenance protein, the condensin. Finally, I present a structural study of a DNA-analogue by thermal shifting essays and single molecule experiments. I included also a technical implementation of a (F-S) combined with TIRF set up to promote the high-speed exchanging buffer for study protein DNA interactions. In the AS single molecule force spectroscopy (SMFS) study, I afford the problem of AS lacking of well defined structure by stretching and unfolding a single polyprotein containing the human AS by employing a SMFS approach. The analysis of the different unfolding pathways gives information about the structural conformation of the protein before the mechanical denaturation. The AS was found to assume three distinct conformational states ranging from a random coil to a highly structured conformation. Since ligands, such as Epigallocatechin-3-Gallate (EGCG) and Dopamine (DA), are known to affect the fibrillation process of AS, I used this single molecule technique to investigate the effect of EGCG and DA on the conformational ensemble of the WT AS. Moreover, knowing from several studies that the presence of point mutations, linked to familial PD, correlate with the gaining of structure and therefore with AS aggregation, I SMFS studies also on AS with three different single point mutations (A30P, A53T and E83A). A particular emphasis was given to the comparison between SMFS results and native mass spectrometry data for the conformational changes of AS in the presence of both DA and EGCG. In the following part, related to the DAP: diaminopurine-substituted DNA, a systematic comparison between a wild-type DNA and DAP DNA is performed, in terms of thermal stability and nanomechanical properties, measured at low and high forces. At low forces the DNA extension and bending rigidity were investigated, by using both MT and AFM, while at high forces the overstretching transition behaviour was explored. In the section related to condensin mediated DNA collapsing, I present a single-molecule MT study to measure, in real-time, the compaction of individual DNA molecules by the condensin complex in the presence of ATP. Since many compaction traces showed sudden distinct decreases in the DNA end-to-end length, I present and validate two different very conservative user-bias-independent step-finding algorithm to extract the size of these compaction steps. Finally, a DNA flow stretching implementation is presented. Briefly, several flow cells were tested to achieve a fast buffer exchange in both MT and F-S coupled with TIRF, in the frame of visualisation of DNA:proteins interactions. We validated our flow cells in term of boundary exchange and applied force. We also visualized fluorescent DNA molecules stretched in the presence of several flow rates.
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Yang, Shilong 1975. "Theoretical study of single-molecule spectroscopy and vibrational spectroscopy in condensed phases." Thesis, Massachusetts Institute of Technology, 2005. http://hdl.handle.net/1721.1/30237.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2005.
Includes bibliographical references (p. 267-279).
In this thesis, theoretical models and computer simulations are employed to study several problems of single-molecule spectroscopy and vibrational spectroscopy in condensed phases. The first part of the thesis concentrates on studying dynamic disorders probed by single molecule fluorescence spectroscopy. Event statistics and correlations of single-molecule fluorescence sequences of modulated reactions are evaluated for multi-channel model, diffusion-controlled reaction model, and stochastic rate model. Several event-related measurements, such as the on-time correlation and the two-event number density, are proposed to map out the memory function, which characterizes the correlation in the conformational fluctuations. A semiflexible Gaussian chain model is used to determine the statistics and correlations of single-molecule fluorescence resonant energy transfer (FRET) experiments on biological polymers. The distribution functions of the fluorescence lifetime and the FRET efficiency provide direct measures of the chain stiffness and their correlation functions probe the intra-chain dynamics at the single-molecule level. The fluorescence lifetime distribution is decomposed into high order memory functions that can be measured in single- molecule experiments. The scaling of the average fluorescence lifetime on the contour length is predicted with the semi-flexible Gaussian chain model and agrees favorably with recent experiments and computer simulations.
(cont.) To interpret the fluorescence measurements of the mechanical properties of double-stranded DNA, a worm-like chain model is used as a first-principle model to study double-stranded DNA under hydrodynamic flows. The second part of the thesis concentrates on nonperturbative vibrational energy relaxation (VER) effects of vibrational line shapes. In general, nonperturbative and non-Markovian VER effects are demonstrated more strongly on nonlinear vibrational line shapes than on linear absorption.
by Shilong Yang.
Ph.D.
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Books on the topic "Single Molecule Spectroscopy (SMS)"

1

Rigler, Rudolf, Michel Orrit, and Thomas Basché. Single Molecule Spectroscopy. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1.

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Rudolf, Rigler, Orrit M. 1956-, and Basché T, eds. Single molecule spectroscopy: Nobel conference lectures. Berlin: Springer, 2001.

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Basché, T., W. E. Moerner, M. Orrit, and U. P. Wild, eds. Single-Molecule Optical Detection, Imaging and Spectroscopy. Weinheim, Germany: VCH Verlagsgesellschaft mbH, 1996. http://dx.doi.org/10.1002/9783527614714.

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Radiom, Milad. Correlation Force Spectroscopy for Single Molecule Measurements. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-14048-3.

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Basché, T. Single-molecule optical detection, imaging and spectroscopy. Weinheim: VCH, 1997.

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Ch, Zander, Enderlein J, and Keller Richard A, eds. Single molecule detection in solution: Methods and applications. Berlin: Wiley-VCH, 2002.

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Gräslund, Astrid, Rudolf Rigler, and Jerker Widengren, eds. Single Molecule Spectroscopy in Chemistry, Physics and Biology. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-02597-6.

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Force and Conductance Spectroscopy of Single Molecule Junctions. [New York, N.Y.?]: [publisher not identified], 2012.

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Oxidative Folding in Bacteria: Studies Using Single Molecule Force Spectroscopy. [New York, N.Y.?]: [publisher not identified], 2016.

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Astrid, Gräslund, Rigler Rudolf, and Widengren Jerker, eds. Single molecule spectroscopy in chemistry, physics and biology: Nobel Symposium. Heidelburg [Germany]: Springer, 2010.

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Book chapters on the topic "Single Molecule Spectroscopy (SMS)"

1

Lebold, Timo, Jens Michaelis, Thomas Bein, and Christoph Bräuchle. "Single Molecule Spectroscopy." In Characterization of Solid Materials and Heterogeneous Catalysts, 585–607. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527645329.ch14.

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Schuler, Benjamin. "Single-Molecule Spectroscopy." In Encyclopedia of Biophysics, 2347–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_604.

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Schleifenbaum, Frank, Christian Blum, Marc Brecht, and Alfred J. Meixner. "Single-Molecule Spectroscopy." In Handbook of Spectroscopy, 821–76. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527654703.ch21.

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Xie, X. S., and H. P. Lu. "Single-Molecule Enzymology." In Single Molecule Spectroscopy, 227–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1_13.

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Dovichi, N. J., R. Polakowski, A. Skelley, D. B. Craig, and J. Wong. "Single-Molecule Enzymology." In Single Molecule Spectroscopy, 241–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1_14.

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Ferrand, Patrick, Jérôme Wenger, and Hervé Rigneault. "Fluorescence Correlation Spectroscopy." In Single Molecule Analysis, 181–95. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-282-3_10.

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Brunel, C., P. Tamarat, B. Lounis, and M. Orrit. "Triggered Emission of Single Photons by a Single Molecule." In Single Molecule Spectroscopy, 99–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1_5.

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Ashkin, A. "History of Optical Trapping and Manipulation of Small Neutral Particles, Atoms, and Molecules." In Single Molecule Spectroscopy, 1–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1_1.

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Rigler, R., L. Edman, Z. Földes-Papp, and S. Wennmalm. "Fluorescence Correlation Spectroscopy in Single-Molecule Analysis: Enzymatic Catalysis at the Single Molecule Level." In Single Molecule Spectroscopy, 177–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1_10.

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Wohland, T., K. Friedrich-Bénet, H. Pick, A. Preuss, R. Hovius, and H. Vogel. "The Characterization of a Transmembrane Receptor Protein by Fluorescence Correlation Spectroscopy." In Single Molecule Spectroscopy, 195–210. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56544-1_11.

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Conference papers on the topic "Single Molecule Spectroscopy (SMS)"

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Orrit, M., and J. Bernard. "Single Molecule Spectroscopy : Photon Correlation And Electric Field Effect." In Spectral Hole-Burning and Luminescence Line Narrowing: Science and Applications. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/shbl.1992.ma3.

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The first single molecule detection, by Moerner and colleagues [1] in the system pentacene in p-terphenyl crystal via absorption, has been extremely difficult due to photon noise. In our paper [2], we demonstrated for the first time single molecule lines in fluorescence excitation spectra of the same system. This much simpler method provides a dramatic improvement of the signal/noise ratio. It opened the way for a true single molecule spectroscopy (SMS). Since then, several experiments performed using this technique [3-8] have shown the power and promise of this new spectroscopic method. In this report, we want to apply SMS to obtain detailed information about individual molecules and the differences in some spectroscopic properties due to their local surroundings. We also report on preliminary results on electric field effects on single molecule lines.
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2

Rebane, Karl K. "Zero-Phonon Line as the Corner Stone of Single Impurity Center Spectroscopy." In Spectral Hole-Burning and Related Spectroscopies: Science and Applications. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/shbs.1994.wb5.

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1. In conventional optical addressing the diffraction limit λ3 selects a body about 1010 molecules to be under illumination. Out of them 104 are impurities, if their relative concentration is 10-6. Single impurity molecule spectroscopy (SMS) has to deal with one molecule at the back-ground of 1010molecules, whose frequencies are out of resonance with the excitation by a few thousands of cm-1 (the host molecules) and 104 molecules in the inhomogeneous impurity band distributed over about 1-1000 cm-1 around the resonance. The single molecule subject to SMS (which is really a spectroscopy, not only detection) must have a sharp and intense absorption line towering well above the spectral background created by the other 1010 molecules under illumination [1,2]. The purely electronic zero-phonon line (ZPL), “the optical analog of the Mossbauer γ-resonance line” ([3] and references therein) is a proper candidate to that role.
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Croci, Mauro, Thomas Irngartinger, Marco Pirotta, Victor Palm, Taras Plakhotnik, W. E. Moerner, Alois Renn, and Urs P. Wild. "Single molecule spectroscopy: measurements of spectral shifts and fluorescence images." In Spectral Hole-Burning and Related Spectroscopies: Science and Applications. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/shbs.1994.wd1.

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Spectral shifts of the molecular resonance frequency have been observed since the early days of single molecule spectroscopy (SMS) [4]. We call these effects for concreteness light-induced spectral shifts (LISS) or spontaneous spectral shifts (SSS or S3) to distinguish the two possible reasons for the spectral change. In order to gain a more complete picture of these effects we have undertaken three different approaches.
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Basché, Th, S. Kummer, R. Kettner, J. Tittel, and C. Bräuchle. "Single Molecule Spectroscopy of Novel Crystalline and Polymeric Systems." In Spectral Hole-Burning and Related Spectroscopies: Science and Applications. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/shbs.1994.wb3.

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Single molecule spectroscopy in solids at low temperature is a very rapidly growing field which due to the sensitivity of a single molecule to its truly local environment yields new insights in the structure and dynamics of crystalline and amorphous solids [1,2]. In the first years of SMS a lot of different experimental techniques have been applied to only a few well selected systems. These were the mixed crystalline system pentacene in p-terphenyl, and perylene and terrylene in poly(ethylene). Very recently, it was recognized by several groups that it is important to find new systems to demonstrate the more general applicability of this new and exciting spectroscopy. While there are several - well known - stringent requirements for any specific system to observe single molecule spectra with the fluorescence excitation technique, recent successful experiments proved that there is still a wide variety of systems where SMS can be pursued. Two new systems introduced lately were terrylene in the Shpol’skii matrix hexadecane [3] and Rhodamine 640 in (poly)ethylene [4]. In our group we investigated new crystalline as well as new polymeric systems.
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Gryczynski, Z., I. Gryczynski, E. G. Matveeva, N. Calander, R. Grygorczyk, I. Akopova, S. Bharill, P. Muthu, S. Klidgar, and J. Borejdo. "New surface plasmons approach to single molecule detection (SMD) and fluorescence correlation spectroscopy (FCS)." In Biomedical Optics (BiOS) 2007, edited by Jorg Enderlein and Zygmunt K. Gryczynski. SPIE, 2007. http://dx.doi.org/10.1117/12.715268.

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Lykke, Keith R., Peter Wurz, Deborah H. Parker, Jerry E. Hunt, Michael J. Pellin, and Dieter M. Gruen. "Molecular Surface Analysis Utilizing Laser Desorption/Laser Ionization." In Laser Applications to Chemical Analysis. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/laca.1992.thb4.

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The ability to analyze surface elemental composition has existed for some time. The various methods include Auger Electron Spectroscopy (AES), Secondary Ion Mass Spectrometry (SIMS), and many more.1 However, molecular surface analysis is only now achieving the same sensitivity and selectivity. Molecular surface analysis often utilizes various optical probes: IR Reflection Absorption Spectroscopy, Sum-Frequency (or Second Harmonic) Generation Spectroscopy on Surfaces, etc. These techniques are generally lacking species-specific information. Another approach is to remove the molecule from the surface and probe it in the gas phase, e.g., with state- of-the-art mass spectrometry. Since mass spectrometry offers high resolution and high sensitivity, the remaining problems are removal of the molecule from the surface and ionization without alteration of the molecule (e.g., fragmentation). These pose serious complications for large molecules, in particular. Furthermore, if the molecule of interest is only a minor constituent of a sample, mass resolution and sensitivity are not sufficient for species identification, and a pre- selection in the ionization is often necessary. Our solution is to employ lasers for both desorption from the sample and ionization (post-ionization) of the gas-phase species. The ability to choose the wavelength and intensity of the desorption laser and the post-ionization laser allows for proper tailoring to the needs of the investigation. This will be demonstrated with two examples. First, a vulcanizate (rubber) will be analyzed with a time-of-flight mass spectrometer for the organic additives present in minor concentrations in the near-surface region. Second, a new class of carbon molecules (fullerenes) will be examined with a Fourier transform mass spectrometer.
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Van Duyne, Richard P., P. M. Champion, and L. D. Ziegler. "Single Molecule and Single Particle SERS." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482687.

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Jaffiol, Rodolphe, and Pascale Winckler. "Single molecule fluorescence saturation spectroscopy." In SPIE BiOS, edited by Jörg Enderlein, Ingo Gregor, Zygmunt K. Gryczynski, Rainer Erdmann, and Felix Koberling. SPIE, 2014. http://dx.doi.org/10.1117/12.2037029.

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Xie, Sunney, and Robert C. Dunn. "Near-field single molecule spectroscopy." In Photonics West '95, edited by Bryan L. Fearey. SPIE, 1995. http://dx.doi.org/10.1117/12.206436.

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Chen, Peng. "SINGLE-MOLECULE MICROSCOPY OF NANOCATALYSIS." In 69th International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2014. http://dx.doi.org/10.15278/isms.2014.ma03.

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Reports on the topic "Single Molecule Spectroscopy (SMS)"

1

Michael Holman, Ling Zang, Ruchuan Liu, and David M. Adams. Single Molecule Spectroscopy of Electron Transfer. Office of Scientific and Technical Information (OSTI), October 2009. http://dx.doi.org/10.2172/966129.

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Ambrose, W. P., T. Basche, and W. E. Moerner. Single Molecule Spectral Diffusion in a Solid Detected Via Fluorescence Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, October 1991. http://dx.doi.org/10.21236/ada243748.

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Van Duyne, Richard. Instrumentation for Atomic Layer Deposition and Single Molecule SERS/TERS Excitation Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, August 2009. http://dx.doi.org/10.21236/ada589757.

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Laurence, Ted Alfred. Photon-counting single-molecule spectroscopy for studying conformational dynamics and macromolecular interactions. Office of Scientific and Technical Information (OSTI), January 2002. http://dx.doi.org/10.2172/813378.

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Hanke, Andreas. Regulation of DNA Metabolism by DNA-Binding Proteins Probed by Single Molecule Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, December 2006. http://dx.doi.org/10.21236/ada459264.

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Ukhanov, Alexander, Gennady Smolyakov, Fei-Hung Chu, Dmitri Tenne, Jeffrey Rack, and Kevin Malloy. DOE SBIR Phase II/IIA Final Report: Atomic Force Microscope Active Optical Probe for Single-Molecule Imaging and Time-Resolved Optical Spectroscopy. Office of Scientific and Technical Information (OSTI), August 2022. http://dx.doi.org/10.2172/1887584.

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Lee, Sang-Hyuk, Shishir Chundawat, Eric Lam, Matthew Lang, Wellington Muchero, and Sai Vankatesh Pingali. In planta single-molecule imaging and holographic force spectroscopy to study real-time, multimodal turnover dynamics of polysaccharides and associated carbohydrate metabolites. Office of Scientific and Technical Information (OSTI), March 2023. http://dx.doi.org/10.2172/1960742.

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