Статті в журналах з теми "Structure and Dynamics of Peptides by NMR Spectroscopy"
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Siminovitch, David J. "Solid-state NMR studies of proteins: the view from static 2H NMR experiments." Biochemistry and Cell Biology 76, no. 2-3 (May 1, 1998): 411–22. http://dx.doi.org/10.1139/o98-054.
Повний текст джерелаAder, C., R. Schneider, K. Seidel, M. Etzkorn, and M. Baldus. "Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 991–95. http://dx.doi.org/10.1042/bst0350991.
Повний текст джерелаHong, Mei. "Structure, Topology, and Dynamics of Membrane Peptides and Proteins from Solid-State NMR Spectroscopy." Journal of Physical Chemistry B 111, no. 35 (September 2007): 10340–51. http://dx.doi.org/10.1021/jp073652j.
Повний текст джерелаPOLYANSKY, ANTON A., PAVEL E. VOLYNSKY, and ROMAN G. EFREMOV. "COMPUTER SIMULATIONS OF MEMBRANE-LYTIC PEPTIDES: PERSPECTIVES IN DRUG DESIGN." Journal of Bioinformatics and Computational Biology 05, no. 02b (April 2007): 611–26. http://dx.doi.org/10.1142/s0219720007002783.
Повний текст джерелаBUCK, MATTHIAS. "Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins." Quarterly Reviews of Biophysics 31, no. 3 (August 1998): 297–355. http://dx.doi.org/10.1017/s003358359800345x.
Повний текст джерелаKrishnan, V. V., Timothy Bentley, Alina Xiong, and Kalyani Maitra. "Conformational Ensembles by NMR and MD Simulations in Model Heptapeptides with Select Tri-Peptide Motifs." International Journal of Molecular Sciences 22, no. 3 (January 29, 2021): 1364. http://dx.doi.org/10.3390/ijms22031364.
Повний текст джерелаJobin, Marie-Lise, Lydie Vamparys, Romain Deniau, Axelle Grélard, Cameron Mackereth, Patrick Fuchs, and Isabel Alves. "Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide." International Journal of Molecular Sciences 20, no. 18 (September 9, 2019): 4441. http://dx.doi.org/10.3390/ijms20184441.
Повний текст джерелаSinelnikova, Anna, and David van der Spoel. "NMR refinement and peptide folding using the GROMACS software." Journal of Biomolecular NMR 75, no. 4-5 (March 28, 2021): 143–49. http://dx.doi.org/10.1007/s10858-021-00363-z.
Повний текст джерелаBechinger, Burkhard. "The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy." Biochimica et Biophysica Acta (BBA) - Biomembranes 1462, no. 1-2 (December 1999): 157–83. http://dx.doi.org/10.1016/s0005-2736(99)00205-9.
Повний текст джерелаO’Connor, Casey, Kate L. White, Nathalie Doncescu, Tatiana Didenko, Bryan L. Roth, Georges Czaplicki, Raymond C. Stevens, Kurt Wüthrich, and Alain Milon. "NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor." Proceedings of the National Academy of Sciences 112, no. 38 (September 8, 2015): 11852–57. http://dx.doi.org/10.1073/pnas.1510117112.
Повний текст джерелаShao, Qing, Kong M. Wong, Dillon T. Seroski, Yiming Wang, Renjie Liu, Anant K. Paravastu, Gregory A. Hudalla та Carol K. Hall. "Anatomy of a selectively coassembled β-sheet peptide nanofiber". Proceedings of the National Academy of Sciences 117, № 9 (18 лютого 2020): 4710–17. http://dx.doi.org/10.1073/pnas.1912810117.
Повний текст джерелаKobchikova, Polina P., Sergey V. Efimov, and Vladimir V. Klochkov. "Binding of Different Cyclosporin Variants to Micelles Evidenced by NMR and MD Simulations." Membranes 13, no. 2 (February 5, 2023): 196. http://dx.doi.org/10.3390/membranes13020196.
Повний текст джерелаHuster, Daniel. "Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR." Progress in Nuclear Magnetic Resonance Spectroscopy 46, no. 2-3 (May 2005): 79–107. http://dx.doi.org/10.1016/j.pnmrs.2005.01.001.
Повний текст джерелаTrzepałka, Emilia, Marta Oleszczuk, Maciej Maciejczyk, and Bernard Lammek. "Solution structure of conformationally restricted vasopressin analogues." Acta Biochimica Polonica 51, no. 1 (March 31, 2004): 33–49. http://dx.doi.org/10.18388/abp.2004_3594.
Повний текст джерелаYOUNG, Helen, Vikram ROONGTA, Thomas J. DALY, and Kevin H. MAYO. "NMR structure and dynamics of monomeric neutrophil-activating peptide 2." Biochemical Journal 338, no. 3 (March 8, 1999): 591–98. http://dx.doi.org/10.1042/bj3380591.
Повний текст джерелаScheidt, Holger A., and Daniel Huster. "Structure and Dynamics of the Myristoyl Lipid Modification of Src Peptides Determined by 2H Solid-State NMR Spectroscopy." Biophysical Journal 96, no. 9 (May 2009): 3663–72. http://dx.doi.org/10.1016/j.bpj.2009.02.028.
Повний текст джерелаBechinger, B. "ChemInform Abstract: The Structure, Dynamics, and Orientation of Antimicrobial Peptides in Membranes by Multidimensional Solid-State NMR Spectroscopy." ChemInform 31, no. 20 (June 8, 2010): no. http://dx.doi.org/10.1002/chin.200020298.
Повний текст джерелаWeber, Daniel K., and Gianluigi Veglia. "A Theoretical Assessment of the Structure Determination of Multi-Span Membrane Proteins by Oriented Sample Solid-State NMR Spectroscopy." Australian Journal of Chemistry 73, no. 3 (2020): 246. http://dx.doi.org/10.1071/ch19307.
Повний текст джерелаKaras, John A., David W. Keizer, and Marc-Antoine Sani. "Nuclear Magnetic Resonance Study of the Peptide FRANCESSEPAROVIC." Australian Journal of Chemistry 73, no. 3 (2020): 158. http://dx.doi.org/10.1071/ch19357.
Повний текст джерелаSinnaeve, Davy, Abir Ben Bouzayene, Emile Ottoy, Gert-Jan Hofman, Eva Erdmann, Bruno Linclau, Ilya Kuprov, José C. Martins, Vladimir Torbeev, and Bruno Kieffer. "Fluorine NMR study of proline-rich sequences using fluoroprolines." Magnetic Resonance 2, no. 2 (November 9, 2021): 795–813. http://dx.doi.org/10.5194/mr-2-795-2021.
Повний текст джерелаWang, Guangshun. "Structure, dynamics and mapping of membrane-binding residues of micelle-bound antimicrobial peptides by natural abundance 13C NMR spectroscopy." Biochimica et Biophysica Acta (BBA) - Biomembranes 1798, no. 2 (February 2010): 114–21. http://dx.doi.org/10.1016/j.bbamem.2009.07.028.
Повний текст джерелаJacob, Maik H., Roy N. D’Souza, Alexandra I. Lazar, and Werner M. Nau. "Diffusion-Enhanced Förster Resonance Energy Transfer in Flexible Peptides: From the Haas-Steinberg Partial Differential Equation to a Closed Analytical Expression." Polymers 15, no. 3 (January 30, 2023): 705. http://dx.doi.org/10.3390/polym15030705.
Повний текст джерелаŻamojć, Krzysztof, Karolina Streńska, Dariusz Wyrzykowski, Lech Chmurzyński та Joanna Makowska. "Interactions of Aβ1-42 Peptide and Its Three Fragments (Aβ8-12, Aβ8-13, and Aβ5-16) with Selected Nonsteroidal Drugs and Compounds of Natural Origin". Symmetry 12, № 10 (23 вересня 2020): 1579. http://dx.doi.org/10.3390/sym12101579.
Повний текст джерелаForneris, Federico, B. Tom Burnley, and Piet Gros. "Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (February 15, 2014): 733–43. http://dx.doi.org/10.1107/s1399004713032549.
Повний текст джерелаGanicz, Katarzyna. "ChemInform Abstract: Solid State NMR Spectroscopy as a Tool for Investigation of Structure and Dynamics of Amino Acids and Model Peptides." ChemInform 31, no. 43 (October 24, 2000): no. http://dx.doi.org/10.1002/chin.200043299.
Повний текст джерелаFritzsch, Jacob, Alexander Korn, Dayana Surendran, Martin Krueger, Holger A. Scheidt, Kaustubh R. Mote, Perunthiruthy K. Madhu, Sudipta Maiti та Daniel Huster. "Probing the Influence of Single-Site Mutations in the Central Cross-β Region of Amyloid β (1–40) Peptides". Biomolecules 11, № 12 (9 грудня 2021): 1848. http://dx.doi.org/10.3390/biom11121848.
Повний текст джерелаPatra, Satyajit, Jean-Benoît Claude, Jean-Valère Naubron, and Jérome Wenger. "Fast interaction dynamics of G-quadruplex and RGG-rich peptides unveiled in zero-mode waveguides." Nucleic Acids Research 49, no. 21 (November 17, 2021): 12348–57. http://dx.doi.org/10.1093/nar/gkab1002.
Повний текст джерелаMetcalf, Douglas G., Joseph M. Kielec, Kathleen G. Valentine, A. Joshua Wand, William F. DeGrado та Joel S. Bennett. "NMR Structure of a Disulfide-Crosslinked αIIbβ3 Cytoplasmic Domain Heterodimer". Blood 112, № 11 (16 листопада 2008): 2866. http://dx.doi.org/10.1182/blood.v112.11.2866.2866.
Повний текст джерелаSzutkowski, Kosma, Emilia Sikorska, Iulia Bakanovych, Amrita Roy Choudhury, Andrej Perdih, Stefan Jurga, Marjana Novič, and Igor Zhukov. "Structural Analysis and Dynamic Processes of the Transmembrane Segment Inside Different Micellar Environments—Implications for the TM4 Fragment of the Bilitranslocase Protein." International Journal of Molecular Sciences 20, no. 17 (August 26, 2019): 4172. http://dx.doi.org/10.3390/ijms20174172.
Повний текст джерелаNguyen, Leonard T., Paulus H. S. Kwakman, David I. Chan, Zhihong Liu, Leonie de Boer, Sebastian A. J. Zaat, and Hans J. Vogel. "Exploring Platelet Chemokine Antimicrobial Activity: Nuclear Magnetic Resonance Backbone Dynamics of NAP-2 and TC-1." Antimicrobial Agents and Chemotherapy 55, no. 5 (February 14, 2011): 2074–83. http://dx.doi.org/10.1128/aac.01351-10.
Повний текст джерелаZhao, Yue, Songyi Lin, Ruiwen Yang, Dong Chen, and Na Sun. "Proton Dynamics of Water Diffusion in Shrimp Hydrolysates Flour and Effects of Moisture Absorption on Its Properties." Foods 10, no. 5 (May 20, 2021): 1137. http://dx.doi.org/10.3390/foods10051137.
Повний текст джерелаSheveleva, Nadezhda N., Irina I. Tarasenko, Mikhail A. Vovk, Mariya E. Mikhailova, Igor M. Neelov, and Denis A. Markelov. "NMR Studies of Two Lysine Based Dendrimers with Insertion of Similar Histidine-Arginine and Arginine-Histidine Spacers Having Different Properties for Application in Drug Delivery." International Journal of Molecular Sciences 24, no. 2 (January 4, 2023): 949. http://dx.doi.org/10.3390/ijms24020949.
Повний текст джерелаVahidi, Siavash, Zev A. Ripstein, Jordan B. Juravsky, Enrico Rennella, Alfred L. Goldberg, Anthony K. Mittermaier, John L. Rubinstein, and Lewis E. Kay. "An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR." Proceedings of the National Academy of Sciences 117, no. 11 (March 2, 2020): 5895–906. http://dx.doi.org/10.1073/pnas.1921630117.
Повний текст джерелаWolff, Martin, Klaus Gast, Andreas Evers, Michael Kurz, Stefania Pfeiffer-Marek, Anja Schüler, Robert Seckler, and Anja Thalhammer. "A Conserved Hydrophobic Moiety and Helix–Helix Interactions Drive the Self-Assembly of the Incretin Analog Exendin-4." Biomolecules 11, no. 9 (September 3, 2021): 1305. http://dx.doi.org/10.3390/biom11091305.
Повний текст джерелаNagy, Tamás Milán, Krisztina Knapp, Eszter Illyés, István Timári, Gitta Schlosser, Gabriella Csík, Attila Borics, Zsuzsa Majer, and Katalin E. Kövér. "Photochemical and Structural Studies on Cyclic Peptide Models." Molecules 23, no. 9 (August 30, 2018): 2196. http://dx.doi.org/10.3390/molecules23092196.
Повний текст джерелаClemente, Joyce S., Edward G. Gregorich, André J. Simpson, Rajeev Kumar, Denis Courtier-Murias, and Myrna J. Simpson. "Comparison of nuclear magnetic resonance methods for the analysis of organic matter composition from soil density and particle fractions." Environmental Chemistry 9, no. 1 (2012): 97. http://dx.doi.org/10.1071/en11096.
Повний текст джерелаPenk, Anja, Matthias Müller, Holger A. Scheidt, Dieter Langosch та Daniel Huster. "Structure and dynamics of the lipid modifications of a transmembrane α-helical peptide determined by 2H solid-state NMR spectroscopy". Biochimica et Biophysica Acta (BBA) - Biomembranes 1808, № 3 (березень 2011): 784–91. http://dx.doi.org/10.1016/j.bbamem.2010.12.015.
Повний текст джерелаHenriques, Sónia Troeira, Evelyne Deplazes, Nicole Lawrence, Olivier Cheneval, Stephanie Chaousis, Marco Inserra, Panumart Thongyoo, et al. "Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7." Journal of Biological Chemistry 291, no. 33 (June 16, 2016): 17049–65. http://dx.doi.org/10.1074/jbc.m116.729095.
Повний текст джерелаvan Well, Renate M., Luciana Marinelli, Cornelis Altona, Kees Erkelens, Gregg Siegal, Mark van Raaij, Antonio L. Llamas-Saiz та ін. "Conformational Analysis of Furanoid ε-Sugar Amino Acid Containing Cyclic Peptides by NMR Spectroscopy, Molecular Dynamics Simulation, and X-ray Crystallography: Evidence for a Novel Turn Structure". Journal of the American Chemical Society 125, № 36 (вересень 2003): 10822–29. http://dx.doi.org/10.1021/ja035461+.
Повний текст джерелаArvidsson, Klas, J�ri Jarvet, Peter Allard, and Anders Ehrenberg. "Solution structure by 1H and dynamics by natural abundance 13C NMR of a receptor recognising peptide derived from a C-terminal fragment of neuropeptide Y." Journal of Biomolecular NMR 4, no. 5 (September 1994): 653–72. http://dx.doi.org/10.1007/bf00404276.
Повний текст джерелаMeredith, Jeffrey J., Antoine Dufour, and Martha D. Bruch. "Comparison of the Structure and Dynamics of the Antibiotic Peptide Polymyxin B and the Inactive Nonapeptide in Aqueous Trifluoroethanol by NMR Spectroscopy." Journal of Physical Chemistry B 113, no. 2 (January 15, 2009): 544–51. http://dx.doi.org/10.1021/jp808379x.
Повний текст джерелаYee, Adelinda A., and Joe D. J. O'Neil. "Uniform nitrogen-15 labeling of a fungal peptide: The structure and dynamics of an alamethicin by nitrogen-15 and proton NMR spectroscopy." Biochemistry 31, no. 12 (March 1992): 3135–43. http://dx.doi.org/10.1021/bi00127a014.
Повний текст джерелаKokubu, Ryoka, Shiho Ohno, Hirohide Kuratani, Yuka Takahashi, Noriyoshi Manabe, Hiroki Shimizu, Yasunori Chiba, et al. "O-Glycan-Dependent Interaction between MUC1 Glycopeptide and MY.1E12 Antibody by NMR, Molecular Dynamics and Docking Simulations." International Journal of Molecular Sciences 23, no. 14 (July 16, 2022): 7855. http://dx.doi.org/10.3390/ijms23147855.
Повний текст джерелаCharretier, E., and M. Guéron. "Application de la résonance magnétique nucléaire à la détermination de la structure des protéines en solution." Biochemistry and Cell Biology 69, no. 5-6 (May 1, 1991): 322–35. http://dx.doi.org/10.1139/o91-051.
Повний текст джерелаBereiter, Raphael, Maximilian Himmelstoß, Eva Renard, Elisabeth Mairhofer, Michaela Egger, Kathrin Breuker, Christoph Kreutz, Eric Ennifar, and Ronald Micura. "Impact of 3-deazapurine nucleobases on RNA properties." Nucleic Acids Research 49, no. 8 (April 15, 2021): 4281–93. http://dx.doi.org/10.1093/nar/gkab256.
Повний текст джерелаDeshmukh, Lalit, Rodolfo Ghirlando, and G. Marius Clore. "Investigation of the Structure and Dynamics of the Capsid-Spacer Peptide 1-Nucleocapsid Fragment of the HIV-1 Gag Polyprotein by Solution NMR Spectroscopy." Angewandte Chemie 126, no. 4 (December 11, 2013): 1043–46. http://dx.doi.org/10.1002/ange.201309127.
Повний текст джерелаDeshmukh, Lalit, Rodolfo Ghirlando, and G. Marius Clore. "Investigation of the Structure and Dynamics of the Capsid-Spacer Peptide 1-Nucleocapsid Fragment of the HIV-1 Gag Polyprotein by Solution NMR Spectroscopy." Angewandte Chemie International Edition 53, no. 4 (December 11, 2013): 1025–28. http://dx.doi.org/10.1002/anie.201309127.
Повний текст джерелаSgourakis, Nikolaos, Andrew C. McShan, Kannan Natarajan, Vlad K. Kumirov, David Flores-Solis, Jiansheng Jiang, Mareike Badstuebner, Evgenii L. Kovrigin, and David H. Margulies. "Chaperone-assisted peptide exchange on MHC-I is driven by a negative allostery release cycle: Implications for a role of peptide-editing Molecular Chaperones in scrutinizing the peptide repertoire." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 99.23. http://dx.doi.org/10.4049/jimmunol.200.supp.99.23.
Повний текст джерелаWang, Jun, Atsushi Tsutsumi, Kiyonobu Yokota, Izuru Kawamura, and Akira Naito. "2A1412 Dynamic structure of antimicrobial peptide alamethicin bound to the acidic lipid bilayers as revealed by solid-state NMR spectroscopy(Biol & Artifi memb 2: Structure & Property, Dynamics, Signal transduction,The 48th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 51, supplement (2011): S73. http://dx.doi.org/10.2142/biophys.51.s73_1.
Повний текст джерелаDeshmukh, Lalit, Rodolfo Ghirlando, and G. Marius Clore. "Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy." Proceedings of the National Academy of Sciences 112, no. 11 (February 23, 2015): 3374–79. http://dx.doi.org/10.1073/pnas.1501985112.
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