Academic literature on the topic 'Force spectroscopy- biological application'

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Journal articles on the topic "Force spectroscopy- biological application"

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Liao, Shuyu, Mengxue Sun, Jinxiu Zhan, Min Xu, and Li Yao. "Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy." Molecules 27, no. 7 (March 23, 2022): 2072. http://dx.doi.org/10.3390/molecules27072072.

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Biomolecules participate in various physiological and pathological processes through intermolecular interactions generally driven by non-covalent forces. In the present review, the force-induced remnant magnetization spectroscopy (FIRMS) is described and illustrated as a novel method to measure non-covalent forces. During the FIRMS measurement, the molecular magnetic probes are magnetized to produce an overall magnetization signal. The dissociation under the interference of external force yields a decrease in the magnetic signal, which is recorded and collected by atomic magnetometer in a spectrum to study the biological interactions. Furthermore, the recent FIRMS development with various external mechanical forces and magnetic probes is summarized.
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Valotteau, Claire, Fidan Sumbul, and Felix Rico. "High-speed force spectroscopy: microsecond force measurements using ultrashort cantilevers." Biophysical Reviews 11, no. 5 (October 2019): 689–99. http://dx.doi.org/10.1007/s12551-019-00585-4.

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Abstract Complete understanding of the role of mechanical forces in biological processes requires knowledge of the mechanical properties of individual proteins and living cells. Moreover, the dynamic response of biological systems at the nano- and microscales span over several orders of magnitude in time, from sub-microseconds to several minutes. Thus, access to force measurements over a wide range of length and time scales is required. High-speed atomic force microscopy (HS-AFM) using ultrashort cantilevers has emerged as a tool to study the dynamics of biomolecules and cells at video rates. The adaptation of HS-AFM to perform high-speed force spectroscopy (HS-FS) allows probing protein unfolding and receptor/ligand unbinding up to the velocity of molecular dynamics (MD) simulations with sub-microsecond time resolution. Moreover, application of HS-FS on living cells allows probing the viscoelastic response at short time scales providing deep understanding of cytoskeleton dynamics. In this mini-review, we assess the principles and recent developments and applications of HS-FS using ultrashort cantilevers to probe molecular and cellular mechanics.
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LI, Hongying, Ningyu GU, and Jilin TANG. "Application of Atomic Force Microscopy Based Single Molecule Force Spectroscopy in Biological Research." Acta Agronomica Sinica 29, no. 12 (2012): 1356. http://dx.doi.org/10.3724/sp.j.1095.2013.20210.

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Carvalho, Filomena A., and Nuno C. Santos. "Atomic force microscopy-based force spectroscopy - biological and biomedical applications." IUBMB Life 64, no. 6 (May 2, 2012): 465–72. http://dx.doi.org/10.1002/iub.1037.

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Wang, Yuchen, Jenny V. Le, Kyle Crocker, Michael A. Darcy, Patrick D. Halley, Dengke Zhao, Nick Andrioff, et al. "A nanoscale DNA force spectrometer capable of applying tension and compression on biomolecules." Nucleic Acids Research 49, no. 15 (August 6, 2021): 8987–99. http://dx.doi.org/10.1093/nar/gkab656.

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Abstract Single molecule force spectroscopy is a powerful approach to probe the structure, conformational changes, and kinetic properties of biological and synthetic macromolecules. However, common approaches to apply forces to biomolecules require expensive and cumbersome equipment and relatively large probes such as beads or cantilevers, which limits their use for many environments and makes integrating with other methods challenging. Furthermore, existing methods have key limitations such as an inability to apply compressive forces on single molecules. We report a nanoscale DNA force spectrometer (nDFS), which is based on a DNA origami hinge with tunable mechanical and dynamic properties. The angular free energy landscape of the nDFS can be engineered across a wide range through substitution of less than 5% of the strand components. We further incorporate a removable strut that enables reversible toggling of the nDFS between open and closed states to allow for actuated application of tensile and compressive forces. We demonstrate the ability to apply compressive forces by inducing a large bend in a 249bp DNA molecule, and tensile forces by inducing DNA unwrapping of a nucleosome sample. These results establish a versatile tool for force spectroscopy and robust methods for designing nanoscale mechanical devices with tunable force application.
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Gabas, Fabio, Riccardo Conte, and Michele Ceotto. "Semiclassical Vibrational Spectroscopy of Biological Molecules Using Force Fields." Journal of Chemical Theory and Computation 16, no. 6 (May 6, 2020): 3476–85. http://dx.doi.org/10.1021/acs.jctc.0c00127.

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Lee, Gil U., Linda Chrisey, and Richard J. Colton. "Measuring forces between biological macromolecules with the Atomic Force Microscope: characterization and applications." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 718–19. http://dx.doi.org/10.1017/s0424820100139962.

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Structure and function in biological macromolecular systems such as proteins and polynucleotides are based on intermolecular interactions that are short ranged and chemically specific. Our knowledge of these molecular interactions results from indirect physical and thermodynamic measurements such as x-ray crystallography, light scattering and nuclear magnetic resonance spectroscopy. Direct measurement of molecular interaction forces requires that the state of a system be monitored with near atomic resolution while an independent force is applied to the system of 10−12 to 10−9 Newton magnitude. The atomic force microscope (AFM) has recently been applied to the study of single molecular interactions. The microfabricated cantilever of the AFM, a force transducer of small yet variable stiffness and high resonance frequency, produces a transducer of 10−15 N/Hz1/2 force sensitivities and 0.01 nm position accuracy.This presentation describes the AFM measurement of the molecular interaction forces in the model ligand-receptor system streptavidin-biotin and between complementary strands of DNA.
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Proksch, Roger, and Sergei Kalinin. "Piezoresponse Force Microscopy." Microscopy Today 17, no. 6 (November 2009): 10–15. http://dx.doi.org/10.1017/s1551929509990988.

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Coupling between electrical and mechanical phenomena is an important feature of functional inorganic materials and biological systems alike. The applications of electromechanically active materials include sonar, ultrasonic and medical imaging, sensors, actuators, and energy-harvesting technologies, as well as non-volatile computer memories. Electromechanical coupling in electromotor proteins and cellular membranes is the universal basis for biological functionalities from hearing to cardiac activity. The future will undoubtedly see the emergence of broad arrays of piezoelectric, biological, and molecular-based electromechanical systems to allow mankind the capability not only to “think” but also “act” on the nanoscale. The need for probing electromechanical functionalities has led to the development of Piezoresponse Force Microscopy (PFM) as a tool for local nanoscale imaging (Figures 1 and 2), spectroscopy, and manipulation of piezoelectric and ferroelectric materials.
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Fisette, Olivier, Patrick Lagüe, Stéphane Gagné, and Sébastien Morin. "Synergistic Applications of MD and NMR for the Study of Biological Systems." Journal of Biomedicine and Biotechnology 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/254208.

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Modern biological sciences are becoming more and more multidisciplinary. At the same time, theoretical and computational approaches gain in reliability and their field of application widens. In this short paper, we discuss recent advances in the areas of solution nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations that were made possible by the combination of both methods, that is, through their synergistic use. We present the main NMR observables and parameters that can be computed from simulations, and how they are used in a variety of complementary applications, including dynamics studies, model-free analysis, force field validation, and structural studies.
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Nandi, Tathagata, and Sri Rama Koti Ainavarapu. "Applications of atomic force microscopy in modern biology." Emerging Topics in Life Sciences 5, no. 1 (February 12, 2021): 103–11. http://dx.doi.org/10.1042/etls20200255.

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Single-molecule force spectroscopy (SMFS) is an emerging tool to investigate mechanical properties of biomolecules and their responses to mechanical forces, and one of the most-used techniques for mechanical manipulation is the atomic force microscope (AFM). AFM was invented as an imaging tool which can be used to image biomolecules in sub-molecular resolution in physiological conditions. It can also be used as a molecular force probe for applying mechanical forces on biomolecules. In this brief review, we will provide exciting examples from recent literature which show how the advances in AFM have enabled us to gain deep insights into mechanical properties and mechanobiology of biomolecules. AFM has been applied to study mechanical properties of cells, tissues, microorganisms, viruses as well as biological macromolecules such as proteins. It has found applications in biomedical fields like cancer biology, where it has been used both in the diagnostic phases as well as drug discovery. AFM has been able to answer questions pertaining to mechanosensing by neurons, and mechanical changes in viruses during infection by the viral particles as well as the fundamental processes such as cell division. Fundamental questions related to protein folding have also been answered by SMFS like determination of energy landscape properties of variety of proteins and their correlation with their biological functions. A multipronged approach is needed to diversify the research, as a combination with optical spectroscopy and computer-based steered molecular dynamic simulations along with SMFS can help us gain further insights into the field of biophysics and modern biology.
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Dissertations / Theses on the topic "Force spectroscopy- biological application"

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Shang, Guangyi. "Development of a shear force scanning near-field optical microscope for biological applications: imaging ans spectroscopy." Reims, 2004. http://www.theses.fr/2004REIMS005.

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Un microscope à champ proche optique basé sur un nouveau senseur de force fonctionnant dans le mode cisaillement a été développé. Il peut être combiné à un microspectrofluorimètre confocal laser pour des applications biologiques et utilisé dans différents modes de fonctionnement. Le mécanisme de détection des forces de cisaillement a été expérimentalement étudié. Il s'avère que l'origine principale de ce mécanisme est le contact intermittent de la sonde avec la surface de l'échantillon qui permet de contrôler la distance pointe-surface. Les paramètres expérimentaux concernant l'imagerie ainsi que les artefacts dus à la géométrie de la sonde sont discutés. Des images en champ proche optique d'un réseau de silicium dans le mode réflexion ainsi que la spectroscopie de structures électroluminescentes dans le mode collection ont été respectivement obtenues. Comme étude préliminaire pour des applications biologiques, la distribution de P-glycoprotéines dans la membrane plasmatique de petites cellules cancéreuses de langue humaine a été étudiée avec une résolution inférieure à la limite de résolution due à la diffraction. Cette distribution n'est pas homogène et se présente sous forme de petits amas. De plus, des spectres de fluorescence ont été obtenus sur des cellules cancéreuses du poumon humain colorées avec la sonde fluorescente JC-1. Des variations dans le spectre de fluorescence ont été mises en évidence avec une résolution verticale de l'ordre de 100 nm. Ces résultats suggèrent que notre système est un outil d'investigation prometteur pour des applications biologiques, capable de fournir des informations dignes d'intérêt permettant de mieux comprendre certains problèmes biologiques
Based on a new force sensor, a shear force scanning near-field optical microscope (ShF-SNOM), that can be operated in the different modes and combined with a confocal laser microspectrofluorometer (CLMF) for biological applications, has been developed. Shear force mechanism was experimentally studied and the knocking mechanism is the main origin responsible for shear force distance control in our system. Experimental parameters concerning the shear force imaging and artifacts due to probe geometric effects are discussed. Shear force and near-field imaging of a silicon grating in the reflection mode, imaging and spectroscopy of electroluminescent structures in the collection mode are demonstrated respectively. As a preliminary study for biological applications, the distribution of P-glycoprotein (P-gp) in the plasma membrane of human small cell lung cancer cells were investigated with sub-diffraction limit resolution. The distribution of P-gp in the cell membrane was found to be not homogenous and cluster formation of P-gp in the membrane was observed. In addition, fluorescence spectra were recorded in a single living cell of human breast adenocarcinoma cells stained with the fluorescent dye JC-1. The variations in fluorescence spectra were measured with vertical resolution of about 100 nm. These results suggest that our system would be a promising tool for biological applications and provide valuable information for understanding some biological problems
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Graham, John Stephen. "Mechanical properties of complex biological systems using AFM-based force spectroscopy." Diss., Columbia, Mo. : University of Missouri-Columbia, 2005. http://hdl.handle.net/10355/4191.

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Thesis (Ph. D.)--University of Missouri-Columbia, 2005.
The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on October 18, 2007) Vita. Includes bibliographical references.
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Klamecka, Kamila [Verfasser], and Heinrich [Akademischer Betreuer] Leonhardt. "Single-molecule force spectroscopy of biological complexes / Kamila Klamecka ; Betreuer: Heinrich Leonhardt." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2017. http://d-nb.info/1156851874/34.

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Ott, Wolfgang Bernhard [Verfasser], and Hermann [Akademischer Betreuer] Gaub. "Single molecule force spectroscopy with biological tools / Wolfgang Bernhard Ott ; Betreuer: Hermann Gaub." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2017. http://d-nb.info/1175878677/34.

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Ferrer, Jorge M. 1976. "Mapping the actin and actin binding proteins interactions : from micromechanics to single molecule force spectroscopy." Thesis, Massachusetts Institute of Technology, 2007. http://hdl.handle.net/1721.1/40950.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Biological Engineering Division, 2007.
Includes bibliographical references.
Mechanical forces play an important role in cell morphology, orientation, migration, adhesion and can even induce apoptosis. The eukaryotic cell is equipped with a dynamic frame, known as the cytoskeleton, that provides the cell's structural integrity in order to sustain and react to such forces. Therefore, understanding the mechanical properties of the cytoskeleton is an important step towards building models describing cell behavior. Filamentous actin (F-actin), as one of the major constituents of the cytoskeleton, has been the target of extensive in vitro studies to determine its mechanical properties in bulk. However, there is still a lack in the understanding of how the molecular interactions between F-actin and the proteins that arrange these filaments into networks regulate the dynamic properties of the cytoskeleton Here we present a novel, single molecule assay to test the rupture force of a complex formed by an actin binding protein (ABP) linking two actin filaments. We readily demonstrate the adaptability of this assay by testing it with two different ABPs: filamin, a crosslinker, and a-actinin, a bundler. We measured rupture forces of 28-73 pN and 30-56 pN for filamin/actin and a-actinin/actin respectively, suggesting that the former is a slightly stronger interaction. Moreover, since no ABP unfolding events were observed at our force levels, our results suggest that ABP unbinding is a more relevant mechanism than unfolding for the temporal regulation of the mechanical properties of the actin cytoskeleton. In addition, we explore the micro-scale properties of F-actin networks reconstituted in vitro.
(cont.) Using imaging and microrheology techniques we characterized the effects of filament length and degree of crosslinking on the structural arrangement and mechanical properties of F-actin networks. We found that the mechanical properties of these networks are length-scale dependent. Also, when probed with active methods, the F-actin networks exhibited strain hardening followed by a gradual softening at forces -30 pN, in good agreement with the single molecule rupture force of 28-73 pN. Thus, with the combination of single molecule and network studies, we can expand the knowledge-base on the regulation and control of the cellular machinery starting from the molecular building blocks.
by Jorge M. Ferrer.
Ph.D.
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Byrne, Katherine. "The viscoelastic response of single biological molecules to thermal noise by atomic force spectroscopy." Thesis, University of Leeds, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.432315.

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Ma, Yong. "THz time domain spectroscopy and its application in biological sciences." Thesis, University of Essex, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.496274.

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Young, Seth Lawton. "Atomic force microscopy probing methods for soft viscoelastic synthetic and biological materials and structures." Diss., Georgia Institute of Technology, 2016. http://hdl.handle.net/1853/54982.

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The focus of this dissertation is on refining atomic force micrscopy (AFM) methods and data analysis routines to measure the viscoelastic mechanical properties of soft polymer and biological materials in relevant fluid environments and in vivo using a range of relevant temperatures, applied forces, and loading rates. These methods are directly applied here to a several interesting synthetic and biological materials. First, we probe poly(n-butyl methacrylate) (PnBMA), above, at and below its glass transition temperature in order to verify our experimental procedure. Next, we use AFM to study the viscoelastic properties of coating materials and additives of silicone-based soft contact lenses in a tear-like saline solution. Finally, a major focus in this dissertation is determining the fundamental mechanical properties that contribute to the excellent sensitivity of the strain sensing organs in a wandering spider (Cupiennius salei) by probing under in vivo conditions. These strain-sensing organs are known to have a significant viscoelastic component. Thus, the cuticle of living spiders is directly investigated in near-natural environments (high humidity, temperatures from 15-40 °C). The main achievements of these studies can be summarized through the following findings: We suggest that full time-temperature-modulus relationships are necessary for the understanding of soft materials systems, and present a practical method for obtaining such relationships. These studies will have a direct impact on both scientists in the metrology field by developing practical experimental procedures and data analysis routines to investigate viscoelastic mechanical properties at the nanoscale, and future materials scientists and engineers by showing via spider mechanosensory systems how viscoelasticity can be applied for functional use in sensing technology.
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Stone, Nicholas. "Raman spectroscopy of biological tissue for application in optical diagnosis of malignancy." Thesis, Cranfield University, 2001. http://dspace.lib.cranfield.ac.uk/handle/1826/4015.

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The utilisation of near-infrared Raman spectroscopy for the discrimination of cancers and pre-cancers from normal tissue in the acro-digestive tract has been evaluated. A commercially available Raman microspectrometer has been modified to provide optimum throughput, sensitivity and fluorescence suppression for epithelial tissue measurements. Laser excitation at 830nm was demonstrated to be optimum. High quality (SN ratio 15-20) NIR-Raman spectra have been acquired from oesophageal and laryngeal tissues in time scales under 30 seconds. Pathological groupings covering the full range of normal and neoplastic tissues in the organs of interest have been studied. Both fresh (snap frozen) and formalin fixed tissue samples were investigated, firstly to indicate whether tissue-types can be distinguished in vivo and secondly to demonstrate the use of Raman spectroscopy as a tool for classification in the pathology lab. Results using multivariate statistical techniques to distinguish between spectra from specimens exhibiting different tissue pathologies have been extremely promising. Cross-validation of the spectral predictive models has shown that three groups of larynx tissue can be separated with sensitivities and specificities of between 86 and 90% and 87 and 95% respectively. Oesophageal prediction models have demonstrated sensitivities and specificities of 84 to 97% and 93 to 98% respectively for a three-group consensus model and 73 to 100% and 92 to 100% for an eight-group consensus model. Epithelial tissues including stomach, tonsil, endometrium, bladder and prostate have been studied to identify further tissues where Raman spectroscopy may be employed for detection of disease. Spectra were similar to those obtained from oesophagus and larynx, although sufficiently different for distinct discriminant models to be required. This work has demonstrated the generic nature of Raman spectroscopy for the detection and classification of cancers and pre-cancerous lesions in many tissues. The evidence provided by this study indicates that utilisation of Raman spectroscopy for non-invasive detection and classification of disease is a distinct possibility. Potential difficulties in the transferability from in vitro to in vivo have been evaluated and no significant barriers have been observed. However, further in vivo probe development and optimisation will be required before 'optical biopsy' with Raman spectroscopy can become a reality.
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D'Entremont, Matthew Ivan. "The application of impedance spectroscopy to assess the viability of biological tissue." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape8/PQDD_0031/MQ63499.pdf.

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Books on the topic "Force spectroscopy- biological application"

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Aleksandr, Noy, ed. Handbook of molecular force spectroscopy. New York, NY: Springer, 2008.

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1951-, Kirste Burkhard, and Lubitz Wolfgang 1949-, eds. Electron nuclear double resonance spectroscopy of radicals in solution: Application to organic and biological chemistry. New York: VCH, 1988.

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Noy, Aleksandr. Handbook of Molecular Force Spectroscopy. Springer, 2010.

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Noy, Aleksandr. Handbook of Molecular Force Spectroscopy. Springer London, Limited, 2007.

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Kurreck, H., B. Kirste, and W. Lubitz. Electron Nuclear Double Resonance Spectroscopy of Radicals in Solution: Application to Organic and Biological Chemistry. Wiley & Sons, Incorporated, John, 1988.

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Book chapters on the topic "Force spectroscopy- biological application"

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Montañez, M. A., J. L. Castro, J. C. Otero, and J. I. Marcos. "SQM Force Field of Glycine: Application to The Analysis of Raman and SERS Spectra." In Spectroscopy of Biological Molecules, 65–66. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_28.

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Tang, Chao, Youjie Fan, and Junhong Lü. "Atomic Force Microscopy-Based Single Molecule Force Spectroscopy for Biological Application." In Atomic Force Microscopy in Molecular and Cell Biology, 29–40. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1510-7_2.

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Hernández, B., A. Hernanz, and R. Navarro. "FT-IR and FT-Raman Spectra of 5’-dAMP. Application of Different Force Fields to Their Assignment." In Spectroscopy of Biological Molecules, 291–92. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_129.

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Durier, V., F. Tristram, and G. Vergoten. "Molecular Force Field Development for Saccharides Using the Spasiba Spectroscopic Potential. Force Field Parameters for Glucose." In Spectroscopy of Biological Molecules, 435. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_199.

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Campos, M., G. Diaz, A. Hernanz, and R. Navarro. "Force Field for 3’-CMP and Vibrational Spectra." In Spectroscopy of Biological Molecules, 287–88. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_127.

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De Grauw, C. J., A. Avogadro, C. Otto, and J. Greve. "Line Scan-Raman Spectroscopy and Atomic Force Microscopy of Chomosomal Banding Patterns." In Spectroscopy of Biological Molecules, 469–70. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_214.

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Gavira, J. M., A. Hernanz, and R. Navarro. "Normal Coordinate Analysis of 5’-CMP. A Comparative Study with Different Force Fields." In Spectroscopy of Biological Molecules, 289–90. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_128.

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Chhiba, M., and G. Vergoten. "Molecular Dynamics Simulations of a Hydrated Phospholipid Bilayer with the Force Field Spasiba." In Spectroscopy of Biological Molecules, 385–86. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_176.

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Bykov, V. A., and V. A. Fedirko. "Scanning Probe Microscopy Application for Biological Objects Investigation." In Spectroscopy of Biological Molecules, 471–72. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_215.

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Leckband, Deborah. "Surface Force Apparatus Measurements of Molecular Forces in Biological Adhesion." In Handbook of Molecular Force Spectroscopy, 1–22. Boston, MA: Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-49989-5_1.

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Conference papers on the topic "Force spectroscopy- biological application"

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Kenkel, Seth, and Rohit Bhargava. "Nanoscale imaging of biological samples with responsivity corrected Atomic Force Microscopy-Infrared (AFM-IR) spectroscopy." In Nanoscale Imaging, Sensing, and Actuation for Biomedical Applications XVI, edited by Dan V. Nicolau, Dror Fixler, and Ewa M. Goldys. SPIE, 2019. http://dx.doi.org/10.1117/12.2510131.

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Weiss, Shimon. "Dual-molecule fluorescence spectroscopy: kinetic observation of single molecule reactions." In Laser Applications to Chemical and Environmental Analysis. Washington, D.C.: Optica Publishing Group, 1998. http://dx.doi.org/10.1364/lacea.1998.lma.6.

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Traditional structural biology ensemble techniques such as x-ray crystallography, electron cryomicroscopy with angular reconstruction, electron microscopy, nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) provide detailed information on the structure of biological macromolecules. In cases where the crystal form of the macromolecule is available, the structure is known with the ultimate atomic resolution. The knowledge of the static structure can provide some insight to the macromolecule function, especially if it is coupled with other biochemical measurements, but in general the structure-function relationship is to a large extent unknown. With the aid of recently developed techniques such as patch clamp, atomic force microscopy (AFM) and optical tweezers, ionic current fluctuations in individual ion channels and forces and/or displacements generated during single molecular motor reaction were measured. Such measurements furnish information about function, but do not provide local, dynamical structural information.
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Asher, Sanford A. "The Potential Revolution of the Free Electron Laser for UV Resonance Raman Spectroscopy in Biological, Structural and Dynamical Studies." In Free-Electron Laser Applications in the Ultraviolet. Washington, D.C.: Optica Publishing Group, 1988. http://dx.doi.org/10.1364/fel.1988.fa1.

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Advances in laser light sources have been the major driving force for progress in the development and application of Raman spectroscopy. The advances have utilized both the increased tunability of the laser sources as well as their short pulse lengths and high peak powers to both increase the information content as well as give dynamical information. We will discuss the revolution in the understanding of molecular and biomolecular structure which will derive from the application of FEL laser sources. We can easily extrapolate the utility of these new sources from our recent extensive UV Raman measurements using state-of-the-art commercial laser sources and non-linear optical conver sion techniques.
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Chae, Inseok, Amira Meddeb, Zoubeida Ounaies, and Seong H. Kim. "Tailoring and Characterization of the Liquid Crystalline Structure of Cellulose Nanocrystals for Opto-Electro-Mechanical Multifunctional Applications." In ASME 2018 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. American Society of Mechanical Engineers, 2018. http://dx.doi.org/10.1115/smasis2018-8016.

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Liquid crystalline (LC) behaviors of cellulose nanocrystal (CNC), derived from wood, cotton or other cellulose-based biopolymers, have been actively investigated due to their unique optical properties and their superb mechanical properties, which open up potential applications in bioelectronics and biomedical engineering. In particular, many attempts have been made to control phase and orientation of LC-CNCs because they are critical factors deciding optical and mechanical properties, and electromechanical performances. Through the applications of mechanical force, electric field and magnetic field, some degree of success has been achieved; however, realizing homogeneous arrangements of CNCs that can be exploited at the macroscale is still elusive, owing to a variety of intermolecular interactions. The characterizations of the LC phase and orientation of CNCs are also challenging due to their complex biological structures. In this report, we introduce approaches to control the phase and orientation of LC-CNCs through the self-assembly, mechanical force and electric field. The liquid crystalline behaviors of CNCs in polar solvents and at the air/water interface are discussed. Translational and rotational behaviors of CNCs under DC electric field are also investigated as a function of their surface charge and dipole moment. In addition, we introduce a nonlinear optical process, namely, sum frequency generation (SFG) spectroscopy, for the structural characterization of LC-CNCs. Using SFG, we can analyze not only crystal phase and structure, but also polar ordering of CNCs which plays a key role in determining their electromechanical performances. Development of cellulose-based smart materials will expand the spectrum of available functional materials that are lightweight, flexible, mechanically tough, and thermally stable at moderately high temperatures (up to 300°C).
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Lian, F. Y., G. F. Jin, and Z. Y. Zhao. "The application of terahertz spectroscopy in studying biological molecules." In International Conference on Environmental Science and Biological Engineering. Southampton, UK: WIT Press, 2014. http://dx.doi.org/10.2495/esbe140601.

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Mieloszyk, Magdalena, Katarzyna Majewska, and Wieslaw Ostachowicz. "THz spectroscopy application for analyzes of internal structure damage due to moisture influence." In Health Monitoring of Structural and Biological Systems XIII, edited by Paul Fromme and Zhongqing Su. SPIE, 2019. http://dx.doi.org/10.1117/12.2513265.

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Sedlacek III, Arthur J., Steven D. Christesen, Tom Chyba, and Pat Ponsardin. "Application of UV-Raman spectroscopy to the detection of chemical and biological threats." In Optical Technologies for Industrial, Environmental, and Biological Sensing, edited by Arthur J. Sedlacek III, Richard Colton, and Tuan Vo-Dinh. SPIE, 2004. http://dx.doi.org/10.1117/12.519165.

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Gong, Justin, John Stanton, and Devin Matthews. "APPLICATION OF FOURTH ORDER VIBRATIONAL PERTURBATION THEORY WITH ANALYTIC HARTREE-FOCK FORCE FIELDS." In 69th International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2014. http://dx.doi.org/10.15278/isms.2014.rc05.

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Salman, A., E. Shufan, I. Lapidot, L. Tsror, L. Zeiri, R. K. Sahu, R. Moreh, S. Mordechai, and M. Huleihel. "Application of multivariate analysis and vibrational spectroscopy in classification of biological systems." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2015 (ICCMSE 2015). AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4938993.

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Liu, Yande, Yibin Ying, Zhongming Chen, and Xiaping Fu. "Application of near-infrared spectroscopy with fiber optics for detecting interior quality in peaches." In Optical Technologies for Industrial, Environmental, and Biological Sensing, edited by Bent S. Bennedsen, Yud-Ren Chen, George E. Meyer, Andre G. Senecal, and Shu-I. Tu. SPIE, 2004. http://dx.doi.org/10.1117/12.533193.

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Reports on the topic "Force spectroscopy- biological application"

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VerMeulen, Holly, Jay Clausen, Ashley Mossell, Michael Morgan, Komi Messan, and Samuel Beal. Application of laser induced breakdown spectroscopy (LIBS) for environmental, chemical, and biological sensing. Engineer Research and Development Center (U.S.), June 2021. http://dx.doi.org/10.21079/11681/40986.

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The Army is interested in sensors capable of characterizing/monitoring the environment (battlefield or military training ranges) at proximal distances. Recently, we evaluated laser induced breakdown spectroscopy (LIBS) systems (hand-held, proximal, and bench top) for the characterization of metals (antimony, copper, lead, tungsten, and zinc) in soils obtained from military training ranges. We then compared the results to findings obtained with standard field and laboratory instrumentation for metals analysis -X-ray Fluorescence (XRF) and Inductively Couple Plasma- Optical Emission Spectroscopy (ICP-OES).
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Phillips, Diana Christine. In Situ Adsorption Studies at the Solid/Liquid Interface:Characterization of Biological Surfaces and Interfaces Using SumFrequency Generation Vibrational Spectroscopy, Atomic Force Microscopy,and Quartz Crystal Microbalance. Office of Scientific and Technical Information (OSTI), January 2006. http://dx.doi.org/10.2172/883802.

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