Relevant bibliographies by topics / Peptide resonance

Academic literature on the topic 'Peptide resonance'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Peptide resonance"

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Martin, Aline, Valentin David, Jennifer S. Laurence, Patricia M. Schwarz, Eileen M. Lafer, Anne-Marie Hedge, and Peter S. N. Rowe. "Degradation of MEPE, DMP1, and Release of SIBLING ASARM-Peptides (Minhibins): ASARM-Peptide(s) Are Directly Responsible for Defective Mineralization in HYP." Endocrinology 149, no. 4 (December 27, 2007): 1757–72. http://dx.doi.org/10.1210/en.2007-1205.

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Mutations in PHEX (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) and DMP1 (dentin matrix protein 1) result in X-linked hypophosphatemic rickets (HYP) and autosomal-recessive hypophosphatemic-rickets (ARHR), respectively. Specific binding of PHEX to matrix extracellular phosphoglycoprotein (MEPE) regulates the release of small protease-resistant MEPE peptides [acidic serine- and aspartate-rich MEPE-associated motif (ASARM) peptides]. ASARM peptides are potent inhibitors of mineralization (minhibins) that also occur in DMP1 [MEPE-related small integrin-binding ligand, N-linked glycoprotein (SIBLING) protein]. It is not known whether these peptides are directly responsible for the mineralization defect. We therefore used a bone marrow stromal cell (BMSC) coculture model, ASARM peptides, anti-ASARM antibodies, and a small synthetic PHEX peptide (SPR4; 4.2 kDa) to examine this. Surface plasmon resonance (SPR) and two-dimensional 1H/15N nuclear magnetic resonance demonstrated specific binding of SPR4 peptide to ASARM peptide. When cultured individually for 21 d, HYP BMSCs displayed reduced mineralization compared with wild type (WT) (−87%, P < 0.05). When cocultured, both HYP and WT cells failed to mineralize. However, cocultures (HYP and WT) or monocultures of HYP BMSCs treated with SPR4 peptide or anti-ASARM neutralizing antibodies mineralized normally. WT BMSCs treated with ASARM peptide also failed to mineralize properly without SPR4 peptide or anti-ASARM neutralizing antibodies. ASARM peptide treatment decreased PHEX mRNA and protein (−80%, P < 0.05) and SPR4 peptide cotreatment reversed this by binding ASARM peptide. SPR4 peptide also reversed ASARM peptide-mediated changes in expression of key osteoclast and osteoblast differentiation genes. Western blots of HYP calvariae and BMSCs revealed massive degradation of both MEPE and DMP1 protein compared with the WT. We conclude that degradation of MEPE and DMP-1 and release of ASARM peptides are chiefly responsible for the HYP mineralization defect and changes in osteoblast-osteoclast differentiation.
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Tsybin, Youri O., Per Håkansson, Magnus Wetterhall, Karin E. Markides, and Jonas Bergquist. "Capillary Electrophoresis and Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for Peptide Mixture and Protein Digest Analysis." European Journal of Mass Spectrometry 8, no. 5 (October 2002): 389–95. http://dx.doi.org/10.1255/ejms.514.

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Recent advances in peptide fragmentation techniques and mass spectrometry have opened up the possibility of combining peptide separation techniques, such as capillary electrophoresis (CE) and capillary liquid chromatography, with Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) and electron capture dissociation (ECD) in order to characterize peptide mixtures and protein digests. The results presented in this study show that CE/ECD-FT-ICR MS can be employed for peptide characterization in mixtures of standard peptides and in peptides resulting from the enzymatic digestion of proteins. Furthermore, the technique has potential for the identification and localization of post-translational modifications in peptides and proteins.
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Vernen, Felicitas, Peta J. Harvey, Susana A. Dias, Ana Salomé Veiga, Yen-Hua Huang, David J. Craik, Nicole Lawrence, and Sónia Troeira Henriques. "Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties." International Journal of Molecular Sciences 20, no. 17 (August 26, 2019): 4184. http://dx.doi.org/10.3390/ijms20174184.

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Tachyplesin I, II and III are host defense peptides from horseshoe crab species with antimicrobial and anticancer activities. They have an amphipathic β-hairpin structure, are highly positively-charged and differ by only one or two amino acid residues. In this study, we compared the structure and activity of the three tachyplesin peptides alongside their backbone cyclized analogues. We assessed the peptide structures using nuclear magnetic resonance (NMR) spectroscopy, then compared the activity against bacteria (both in the planktonic and biofilm forms) and a panel of cancerous cells. The importance of peptide-lipid interactions was examined using surface plasmon resonance and fluorescence spectroscopy methodologies. Our studies showed that tachyplesin peptides and their cyclic analogues were most potent against Gram-negative bacteria and melanoma cell lines, and showed a preference for binding to negatively-charged lipid membranes. Backbone cyclization did not improve potency, but improved peptide stability in human serum and reduced toxicity toward human red blood cells. Peptide-lipid binding affinity, orientation within the membrane, and ability to disrupt lipid bilayers differed between the cyclized peptide and the parent counterpart. We show that tachyplesin peptides and cyclized analogues have similarly potent antimicrobial and anticancer properties, but that backbone cyclization improves their stability and therapeutic potential.
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Wilson, David, and Norelle L. Daly. "Nuclear Magnetic Resonance seq (NMRseq): A New Approach to Peptide Sequence Tags." Toxins 10, no. 11 (October 28, 2018): 437. http://dx.doi.org/10.3390/toxins10110437.

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Structural analysis of peptides with nuclear magnetic resonance (NMR) spectroscopy generally relies on knowledge of the primary sequence to enable assignment of the resonances prior to determination of the three-dimensional structure. Resonance assignment without knowledge of the sequence is complicated by redundancy in amino acid type, making complete de novo sequencing using NMR spectroscopy unlikely to be feasible. Despite this redundancy, we show here that NMR spectroscopy can be used to identify short sequence tags that can be used to elucidate full-length peptide sequences via database searching. In the current study, we have used this approach to identify conotoxins from the venom of the cone snail Conus geographus and determined the three-dimensional structure of a member of the I3 superfamily. This approach is most likely to be useful for the characterization of disulfide-rich peptides, such as those that were chosen for this study, as they generally have well-defined structures, which enhances the quality of the NMR spectra. In contrast to other sequencing methods, the lack of sample manipulation, such as protease digestion, allows for subsequent bioassays to be carried out using the native sample used for sequence identification.
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Syryamina, Victoria N., Alvaro S. Siano, Fernando Formaggio, and Marta De Zotti. "A Peptide-Based Trap for Metal Ions Studied by Electron Paramagnetic Resonance." Chemosensors 10, no. 2 (February 10, 2022): 71. http://dx.doi.org/10.3390/chemosensors10020071.

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Peptide-based materials provide a versatile platform for sensing and ion sequestration since peptides are endowed with stimuli-responsive properties. The mechanism of molecular sensing is often based on peptide structural changes (or switching), caused by the binding of the target molecule. One scope of sensing applications is the selection of a specific analyte, which may be achieved by adjusting the structure of the peptide binding site. Therefore, exact knowledge of peptide properties and 3D-structure in the ‘switched’ state is desirable for tuning the detection and for further molecular construction. Hence, here we demonstrate the performance of Electron Paramagnetic Resonance (EPR) spectroscopy in the identification of metal ion binding by the antimicrobial peptide trichogin GA IV. Na(I), Ca(II), and Cu(II) ions were probed as analytes to evaluate the impact of coordination number, ionic radii, and charge. Conclusions drawn by EPR are in line with literature data, where other spectroscopic techniques were exploited to study peptide-ion interactions for trichogin GA IV, and the structural switch from an extended helix to a hairpin structure, wrapped around the metal ion upon binding of divalent cations was proposed.
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Park, Sunghyouk, Michael E. Johnson, and Leslie W. M. Fung. "Nuclear magnetic resonance studies of mutations at the tetramerization region of human alpha spectrin." Blood 100, no. 1 (July 1, 2002): 283–88. http://dx.doi.org/10.1182/blood.v100.1.283.

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Abstract Many spectrin mutations that destabilize tetramer formation and lead to hereditary hemolytic anemias are located at the N-terminal region of α-spectrin, with the Arg28 position considered to be a mutation hot spot. We have introduced mutations at positions 28 and 45 into a model peptide, Spα1-156, consisting of the first 156 residues in the N-terminal region of α-spectrin (αN). The association of these α-spectrin peptides that have single amino acid replacements with a β-spectrin model peptide, consisting of the C-terminal region of β-spectrin (βC), was determined, and structural changes due to amino acid replacements were monitored by nuclear magnetic resonance (NMR). We found evidence for similar and very localized structural changes in Spα1-156Arg45Thr and Spα1-156Arg45Ser, although these 2 mutant peptides associated with β-spectrin peptide with significantly differing affinities. The Spα1-156Arg28Ser peptide showed an affinity for the β-spectrin peptide comparable to that of Spα1-156Arg45Ser, but it exhibited substantial and widespread spectral changes. Our results suggest that both Arg45 replacements induce only minor structural perturbations in the first helix of Spα1-156, but the Arg28Ser replacement affects both the first helix and the following structural domain. Our results also indicate that the mechanism for reduced spectrin tetramerization is through mutation-induced changes in molecular recognition at the αβ-tetramerization site, rather than through conformational disruption, as has been suggested in prior literature.
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Xia, Ning, Gang Liu, and Xinyao Yi. "Surface Plasmon Resonance for Protease Detection by Integration of Homogeneous Reaction." Biosensors 11, no. 10 (September 29, 2021): 362. http://dx.doi.org/10.3390/bios11100362.

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The heterogeneous assays of proteases usually require the immobilization of peptide substrates on the solid surface for enzymatic hydrolysis reactions. However, immobilization of peptides on the solid surface may cause a steric hindrance to prevent the interaction between the substrate and the active center of protease, thus limiting the enzymatic cleavage of the peptide. In this work, we reported a heterogeneous surface plasmon resonance (SPR) method for protease detection by integration of homogeneous reaction. The sensitivity was enhanced by the signal amplification of streptavidin (SA)-conjugated immunoglobulin G (SA-IgG). Caspase-3 (Cas-3) was determined as the model. A peptide labeled with two biotin tags at the N- and C-terminals (bio-GDEVDGK-bio) was used as the substrate. In the absence of Cas-3, the substrate peptide was captured by neutravidin (NA)-covered SPR chip to facilitate the attachment of SA-IgG by the avidin-biotin interaction. However, once the peptide substrate was digested by Cas-3 in the aqueous phase, the products of bio-GDEVD and GK-bio would compete with the substrate to bond NA on the chip surface, thus limiting the attachment of SA-IgG. The method integrated the advantages of both heterogeneous and homogeneous assays and has been used to determine Cas-3 inhibitor and evaluate cell apoptosis with satisfactory results.
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Lupaescu, Ancuta-Veronica, Cosmin Stefan Mocanu, Gabi Drochioiu, and Catalina-Ionica Ciobanu. "Zinc Binding to NAP-Type Neuroprotective Peptides: Nuclear Magnetic Resonance Studies and Molecular Modeling." Pharmaceuticals 14, no. 10 (October 1, 2021): 1011. http://dx.doi.org/10.3390/ph14101011.

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Aggregation of amyloid-β peptides (Aβ) is a hallmark of Alzheimer’s disease (AD), which is affecting an increasing number of people. Hence, there is an urgent need to develop new pharmaceutical treatments which could be used to prevent the AD symptomatology. Activity-dependent neuroprotective protein (ADNP) was found to be deficient in AD, whereas NAP, an 8-amino-acid peptide (1NAPVSIPQ8) derived from ADNP, was shown to enhance cognitive function. The higher tendency of zinc ion to induce Aβ aggregation and formation of amorphous aggregates is also well-known in the scientific literature. Although zinc binding to Aβ peptides was extensively investigated, there is a shortage of knowledge regarding the relationship between NAP peptide and zinc ions. Therefore, here, we investigated the binding of zinc ions to the native NAP peptide and its analog obtained by replacing the serine residue in the NAP sequence with tyrosine (1NAPVYIPQ8) at various molar ratios and pH values by mass spectrometry (MS) and nuclear magnetic resonancespectroscopy (NMR). Matrix-assisted laser desorption/ionization time-of-flight (MALDI ToF) mass spectrometry confirmed the binding of zinc ions to NAP peptides, while the chemical shift of Asp1, observed in 1H-NMR spectra, provided direct evidence for the coordinating role of zinc in the N-terminal region. In addition, molecular modeling has also contributed largely to our understanding of Zn binding to NAP peptides.
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Nagaraj, G., M. V. Uma, M. S. Shivayogi, and Hemalatha Balaram. "Antimalarial Activities of Peptide Antibiotics Isolated from Fungi." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 145–49. http://dx.doi.org/10.1128/aac.45.1.145-149.2001.

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ABSTRACT Malaria caused by Plasmodium falciparum is a major public health problem in the developing countries of the world. Clinical treatment of malaria has become complicated due to the occurrence of infections caused by drug resistant parasites. Secondary metabolites from fungi are an attractive source of chemotherapeutic agents. This work reports the isolation and in vitro antiplasmodial activities of peptide antibiotics of fungal origin. The three peptide antibiotics used in this study were efrapeptins, zervamicins, and antiamoebin. The high-performance liquid chromatography-purified peptides were characterized by nuclear magnetic resonance and mass spectral analysis. All three fungal peptides kill P. falciparum in culture with 50% inhibitory concentrations in the micromolar range. A possible mode of action of these peptide antibiotics on P. falciparum is presented.
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Kim, Minseon, and Yongae Kim. "Structural Studies of Expressed tIK, Anti-Inflammatory Peptide." International Journal of Molecular Sciences 24, no. 1 (December 30, 2022): 636. http://dx.doi.org/10.3390/ijms24010636.

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Cytokine imbalance is one of the causes of inflammation. Inflammation has yet to be adequately treated without side effects. Therefore, we tried to develop a peptide drug with minimal side effects. Peptide drugs have the advantage of being bio-friendly and bio-specific. In a previous study, three peptides with anti-inflammatory activity were derived based on a truncated IK (tIK) protein, which was a fragment of the IK protein with anti-inflammatory effects. The objective of this study was to optimize the process of expressing, isolating, and purifying the three peptides using bacterial strains and describe the process. Circular dichroism and solution state nuclear magnetic resonance spectroscopy were performed on the final purified high-purity peptide and its secondary structure was also identified.
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Dissertations / Theses on the topic "Peptide resonance"

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Costa, Philip R. (Philip Remi). "Spins, peptides, and Alzheimer's disease : solid-state nuclear magnetic resonance investigations of amyloid peptide conformation." Thesis, Massachusetts Institute of Technology, 1996. http://hdl.handle.net/1721.1/10714.

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Mozsolits, Henriette 1971. "Surface plasmon resonance spectroscopy for the study of peptide-membrane interactions." Monash University, Dept. of Biochemistry and Molecular Biology, 2001. http://arrow.monash.edu.au/hdl/1959.1/8123.

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Thirumoorthy, Ramanan. "NMR studies of structure and dynamics of novel peptide-based melanocortin receptor antagonists." [Gainesville, Fla.] : University of Florida, 2002. http://purl.fcla.edu/fcla/etd/UFE1001186.

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Drew, Daniel L. Jr. "Investigating the Structure and Dynamic Properties of Bacteriophage S21 Pinholin Using Solid-State Nuclear Magnetic Resonance and Electron Paramagnetic Resonance Spectroscopy." Miami University / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=miami1610187893016095.

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Smith, K. I. "The two-dimensional nuclear magnetic resonance spectroscopy analysis of peptides in solution." Thesis, University of Manchester, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.377720.

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Brown, Peter N. "Biophysical and structural characterisation of protein-peptide interactions." Thesis, University of Edinburgh, 2010. http://hdl.handle.net/1842/3982.

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Proliferating cell nuclear antigen (PCNA) is an essential protein in the cell. It is involved in transcription and many types of DNA repair and replication. Homologues of this protein are found in all orders of life. The high level of conservation and essential nature of PCNA infers that it may be a potential drug target for anti-caner drugs in humans and also a potential anti-parasitic target. X-ray structures of PCNA from Homo sapiens (Hs), Schizosaccharomyces pombe (Sp) and Leishmania major (Lm) are now available and can be used as a template for structure based drug design. In this work PCNA from these three species have been prepared in milligram quantities for biochemical and biophysical studies. The previously unknown structure of LmPCNA has been solved in an uncomplexed form and also complexed with a dodecapeptide to a resolution of 3.0Å. A comparison of PCNA structures and their peptide complexes for the three species identifies structural differences which may be relevant in analysing thermodynamic contributions of binding. All eukaryotic PCNA molecules exist as ring shaped trimers which form around DNA. In this work the oligomeric state of LmPCNA has been determined to be hexameric both in solution and in the crystal. It has also been hypothesised that HsPCNA is hexameric however these would seem to form hexamers in which the trimeric rings associate “back-to-back” while LmPCNA trimers would seem to associate “face-to-face”. The binding affinities for these three PCNAs have been determined with a selection of peptides derived from the Hs p21 protein. This work has shown, using a selection of different techniques including Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC) and Dynamic Scanning Fluorimetry (DSF); that HsPCNA and SpPCNA have similar affinities for a 12mer peptide (Kd of ~1μM) however LmPCNA shows significantly weaker interactions (Kd of ~10μM). This is most likely due to divergence in the sequence and structure of LmPCNA. A systematic investigation by SPR on the effect of peptide linker length on binding has been carried out using a series of synthesised peptides with different lengths of chemical spacer. The series of streptavidin immobilised peptides show that longer spacers are required for the recovery of the PCNA peptide binding affinity. The results presented in this work indicate that a linker length of at least 20Å is required for measurable protein binding activity. This interaction is improved with longer peptide spacers.
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DUPONT-QUENET, BEATRICE. "Etude par resonance magnetique nucleaire du peptide a13g. Recherche de l'interaction avec l'alprenolol." Paris 6, 1994. http://www.theses.fr/1994PA066358.

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Le peptide a13g est la representation synthetique d'une region determinante d'un anticorps anti-alprenolol: 37a4. Dans le but de confirmer l'interaction entre ces deux molecules, nous avons observe, par resonance magnetique nucleaire, le comportement du peptide seul et en presence d'alprenolol, en solution aqueuse. L'attribution complete du spectre proton et partielle en carbone a ete realisee. Nous avons constate, qu'a ph acide, celui-ci s'hydrolysait au bout de 5 jours au niveau de la liaison asp-pro. L'etude conformationnelle n'a pas permis de mettre en evidence une structure secondaire reguliere du peptide. Seule, la configuration trans des deux liaisons x-pro a pu etre demontree. Le peptide presente les memes caracteristiques lorsqu'il est en presence d'alprenolol. L'etude de l'interaction, a travers des mesures d'effets overhauser nucleaires intermoleculaires et de temps de relaxation des protons de l'alprenolol, a montre que l'alprenolol ne reconnaissait pas le peptide a13g. Ce dernier serait une representation trop restreinte de l'anticorps anti-alprenolol
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Neidigh, Jonathan Wesley. "Chemical shift tools in peptide folding and miniature protein design /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/8701.

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Francart, Céline. "Etude par resonance magnetique nucleaire de polypeptides contenant plusieurs prolines." Lille 2, 1997. http://www.theses.fr/1997LIL2P269.

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PRECHEUR-AGULHON, BENEDICTE. "Etudes conformationnelles par resonance magnetique nucleaire et par dichroisme circulaire de peptide d'interet biologique." Paris 11, 1993. http://www.theses.fr/1993PA112345.

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Dans une premiere etude j'ai entrepris l'analyse conformationnelle de peptides issus du domaine d'interaction des adenylates cyclases de bordetella pertussis et de bacillus anthracis, avec la calmoduline. Les resultats obtenus suggerent que chacun de ces peptides a tendance a se replier en helice- amphiphile basique, proposee comme motif structural pour l'interaction avec la calmoduline. Afin de confirmer ce modele d'interaction, j'ai entrepris l'etude conformationnelle d'un peptide modele construit pour former une helice- amphiphile basique. L'analyse combinee des experiences rmn homo- et heteronucleaires ont de plus permis l'identification du site d'interaction sur la calmoduline. Dans une seconde etude nous avons caracteriser la conformation d'un peptide antigenique de echinococcus granulosus. Les donnees spectroscopiques obtenues sur le peptide suggerent fortement la presence de trois tours d'helice-. Nous avons tente de stabiliser l'organisation helicoidale du peptide afin d'augmenter l'activite biologique. Toutefois, les etudes conjointes par rmn et par dc montrent que la stabilisation helicoidale est fortement reduite
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Books on the topic "Peptide resonance"

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Naito, Akira, Philip Williamson, Frances Separovic, Robert Tycko, and Yoshitaka Ishii. Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides. Royal Society of Chemistry, The, 2014.

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Carr, Scott R. Gas-phase reactions of amino acids and small peptides as studied in a Fourier transform ion cyclotron resonance mass spectrometer. 1997.

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Carr, Scott R. Gas-phase reactions of amino acids and small peptides as studied in a Fourier transform ion cyclotron resonance mass spectrometer. 1997.

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Palmblad, Magnus. Identification & Characterization of Peptides & Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry (Comprehensive Summaries of ... the Faculty Science and Technology, 706). Uppsala Universitet, 2002.

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Book chapters on the topic "Peptide resonance"

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Strandberg, Erik, and Anne S. Ulrich. "Solid-State NMR for Studying Peptide Structures and Peptide-Lipid Interactions in Membranes." In Modern Magnetic Resonance, 1–13. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-28275-6_114-1.

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Strandberg, Erik, and Anne S. Ulrich. "Solid-State NMR for Studying Peptide Structures and Peptide-Lipid Interactions in Membranes." In Modern Magnetic Resonance, 1985–96. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-28388-3_114.

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Tsvetkov, Yuri D., Michael K. Bowman, and Yuri A. Grishin. "PELDOR in Peptide Research." In Pulsed Electron–Electron Double Resonance, 133–59. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-030-05372-7_6.

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Norton, Raymond S. "Peptide Toxin Structure and Function by NMR." In Modern Magnetic Resonance, 1–18. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-28275-6_120-1.

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Norton, Raymond S. "Peptide Toxin Structure and Function by NMR." In Modern Magnetic Resonance, 2081–97. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-28388-3_120.

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Armitage, Bruce A. "Analysis of PNA Hybridization by Surface Plasmon Resonance." In Peptide Nucleic Acids, 159–65. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-553-8_13.

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Drijfhout, J. W., D. J. v. d. Heuvel, W. Bloemhoff, G. W. Welling, and R. P. H. Kooyman. "An improved method to study peptide-protein interaction by surface plasmon resonance (SPR)." In Peptides, 936–37. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_314.

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Beusen, Denise D., William C. Hutton, John J. Kotyk, Janusz Zabrocki, Miroslaw T. Leplawy, and Garland R. Marshall. "13C and 1H resonance assignments and structural determination of an emerimicin peptide in DMSO." In Peptides 1990, 545–47. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_229.

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Real-Fernández, Feliciana, Giada Rossi, Filomena Panza, Federico Pratesi, Paola Migliorini, and Paolo Rovero. "Surface Plasmon Resonance Method to Evaluate Anti-citrullinated Protein/Peptide Antibody Affinity to Citrullinated Peptides." In Methods in Molecular Biology, 267–74. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2999-3_23.

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Nakamura, Akira, and Norikazu Ueyama. "Chemical Functions of Single and Double NH---S Hydrogen Bond in Iron-Sulfur Metalloproteins; Model Ligands with Cys-containing Peptide and Simple Acylaminobenzenethiolate." In Nuclear Magnetic Resonance of Paramagnetic Macromolecules, 265–79. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-015-8573-6_12.

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Conference papers on the topic "Peptide resonance"

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Bjørlie, Mads, Rachel Irankunda, Jean-Michel Girardet, Sandrine Boschi-Müller, Betül Yesiltas, Charlotte Jacobsen, and Laetitia Canabady-Rochelle. "Screening of Metal-chelating Peptides and Hydrolysates Using Surface Plasmon Resonance and Switchsense." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zszk2778.

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Abstract: Lipid oxidation is, among other factors, catalyzed by the presence of metal ions and efficient metal chelators are therefore highly sought after in the food industry. Among these, natural metal chelators are gaining interest as opposed to their synthetic counterparts such as EDTA. Traditional screening for metal chelation capacity is time consuming and non-specific. The aim of this study was to screen potato protein hydrolysate and synthetic peptides derived from potato protein sequences for their metal-chelating capacity. Seven peptides and two hydrolysates (raw and ultra-filtrated) were studied. Peptides were selected using two different models: an empirical-based bioinformatics approach (AnOxPePred) and a theoretically based model for metal chelation. Surface Plasmon Resonance (SPR) is a label-free, optical technique used to determine the dissociation constant (KD) of a complex formed between immobilized Ni2+ and peptides. The SwitchSENSE technology is another approach used to study Ni2+/peptide affinity. It utilizes the quenching of fluorescence of a fluorophore upon Ni2+ immobilization and the inverse fluorescence increase upon peptide binding onto Ni2+. Both analyses were carried out at pH 7.4. In this study, we successfully determined the dissociation constants (KD) of two peptides (ASH and DHGPKIFEPS) using SPR. These values compare favourably with previous results indicating metal chelating potential. The association rate constant (kon) of all peptides were determined using switchSENSE. Yet, due to bad fitting of the kinetics data obtained with switchSENSE, the KDs of the hydrolysates were only determined with low accuracy.
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Asher, S., B. Sharma, L. Ma, S. Bykov, N. Myshakina, Z. Hong, K. Xiong, P. M. Champion, and L. D. Ziegler. "UV Resonance Raman Investigations of Peptide∕Protein Conformation and Folding." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482445.

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Ishibashi, Jun, Ai Asaoka, Takashi Iwasaki, Hideaki Suzuki, Tomio Nagano, Makoto Nakamura, Mitsuhiro Miyazawa, and Minoru Yamakawa. "Surface Plasmon Resonance Analysis of Beetle Defensin-Derived Antimicrobial Peptide-Membrane Interactions." In The Twenty-Third American and the Sixth International Peptide Symposium. Prompt Scientific Publishing, 2013. http://dx.doi.org/10.17952/23aps.2013.052.

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Ksenevich, Tatiana I., Sergei I. Rogov, Maxim N. Zmak, Maya A. Kupriyanova, Dmitrii V. Klinov, Sergey A. Grachev, and Petr I. Nikitin. "Novel peptide matrix for immobilization of biomolecules for surface plasmon resonance sensing." In Photonics East '99, edited by Mahmoud Fallahi and Basil I. Swanson. SPIE, 1999. http://dx.doi.org/10.1117/12.372918.

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DeBlase, Andrew, Timothy Zwier, Scott McLuckey, Patrick Walsh, and Christopher Harrilal. "IR-UV DOUBLE RESONANCE SPECTROSCOPY OF A COLD PROTONATED FIBRIL-FORMING PEPTIDE: NNQQNY·H+." In 71st International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2016. http://dx.doi.org/10.15278/isms.2016.wi02.

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Bratcher, Amber R., Laurie B. Connell, and Paul Millard. "Portable biosensor detection of the harmful dinoflagellate Alexandrium using surface plasmon resonance and peptide nucleic acid probes." In OCEANS 2011. IEEE, 2011. http://dx.doi.org/10.23919/oceans.2011.6107116.

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Bratcher, Amber R., Laurie B. Connell, and Rosemary L. Smith. "Development of a direct detection method for Alexandrium spp. Using surface plasmon resonance and peptide nucleic acid probes." In 2009 IEEE Sensors. IEEE, 2009. http://dx.doi.org/10.1109/icsens.2009.5398359.

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Hong, Zhenmin, Sanford Asher, P. M. Champion, and L. D. Ziegler. "Dependence of Ethylguanidinium UV Resonance Raman Spectra on the Environment: Insights into the Arginine Sidechain in Peptide and Protein." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482857.

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Harrilal, Christopher, Timothy Zwier, Scott McLuckey, and Anthony Pitts-McCoy. "INVESTIGATING ELECTRONIC AND STRUCTURAL CHANGES IMPOSED BY ZWITTERIONIC PARING IN MODEL PEPTIDE SYSTEMS USING IR-UV-IR TRIPLE RESONANCE SPECTROSCOPY." In 73rd International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2018. http://dx.doi.org/10.15278/isms.2018.fe02.

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Harrilal, Christopher, Timothy Zwier, Scott McLuckey, and Anthony Pitts-McCoy. "THE ROLE OF TYROSINE IN STABILIZING GAS PHASE ZWITTERIONIC CONFIGURATIONS OF PEPTIDE IONS REVEALED BY IR-UV DOUBLE RESONANCE SPECTROSCOPY." In 74th International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2019. http://dx.doi.org/10.15278/isms.2019.tj09.

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Reports on the topic "Peptide resonance"

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Pease, J. Structures of peptide families by nuclear magnetic resonance spectroscopy and distance geometry. Office of Scientific and Technical Information (OSTI), December 1989. http://dx.doi.org/10.2172/7003404.

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Heller, Jonathan. Solid state nuclear magnetic resonance studies of prion peptides and proteins. Office of Scientific and Technical Information (OSTI), August 1997. http://dx.doi.org/10.2172/6428.

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