Artículos de revistas sobre el tema "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, n.º 2-3 (1 de mayo de 1998): 411–22. http://dx.doi.org/10.1139/o98-054.
Texto completoAder, C., R. Schneider, K. Seidel, M. Etzkorn y M. Baldus. "Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers". Biochemical Society Transactions 35, n.º 5 (25 de octubre de 2007): 991–95. http://dx.doi.org/10.1042/bst0350991.
Texto completoHong, Mei. "Structure, Topology, and Dynamics of Membrane Peptides and Proteins from Solid-State NMR Spectroscopy". Journal of Physical Chemistry B 111, n.º 35 (septiembre de 2007): 10340–51. http://dx.doi.org/10.1021/jp073652j.
Texto completoPOLYANSKY, ANTON A., PAVEL E. VOLYNSKY y ROMAN G. EFREMOV. "COMPUTER SIMULATIONS OF MEMBRANE-LYTIC PEPTIDES: PERSPECTIVES IN DRUG DESIGN". Journal of Bioinformatics and Computational Biology 05, n.º 02b (abril de 2007): 611–26. http://dx.doi.org/10.1142/s0219720007002783.
Texto completoBUCK, MATTHIAS. "Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins". Quarterly Reviews of Biophysics 31, n.º 3 (agosto de 1998): 297–355. http://dx.doi.org/10.1017/s003358359800345x.
Texto completoKrishnan, V. V., Timothy Bentley, Alina Xiong y Kalyani Maitra. "Conformational Ensembles by NMR and MD Simulations in Model Heptapeptides with Select Tri-Peptide Motifs". International Journal of Molecular Sciences 22, n.º 3 (29 de enero de 2021): 1364. http://dx.doi.org/10.3390/ijms22031364.
Texto completoJobin, Marie-Lise, Lydie Vamparys, Romain Deniau, Axelle Grélard, Cameron Mackereth, Patrick Fuchs y Isabel Alves. "Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide". International Journal of Molecular Sciences 20, n.º 18 (9 de septiembre de 2019): 4441. http://dx.doi.org/10.3390/ijms20184441.
Texto completoSinelnikova, Anna y David van der Spoel. "NMR refinement and peptide folding using the GROMACS software". Journal of Biomolecular NMR 75, n.º 4-5 (28 de marzo de 2021): 143–49. http://dx.doi.org/10.1007/s10858-021-00363-z.
Texto completoBechinger, Burkhard. "The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy". Biochimica et Biophysica Acta (BBA) - Biomembranes 1462, n.º 1-2 (diciembre de 1999): 157–83. http://dx.doi.org/10.1016/s0005-2736(99)00205-9.
Texto completoO’Connor, Casey, Kate L. White, Nathalie Doncescu, Tatiana Didenko, Bryan L. Roth, Georges Czaplicki, Raymond C. Stevens, Kurt Wüthrich y 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, n.º 38 (8 de septiembre de 2015): 11852–57. http://dx.doi.org/10.1073/pnas.1510117112.
Texto completoShao, Qing, Kong M. Wong, Dillon T. Seroski, Yiming Wang, Renjie Liu, Anant K. Paravastu, Gregory A. Hudalla y Carol K. Hall. "Anatomy of a selectively coassembled β-sheet peptide nanofiber". Proceedings of the National Academy of Sciences 117, n.º 9 (18 de febrero de 2020): 4710–17. http://dx.doi.org/10.1073/pnas.1912810117.
Texto completoKobchikova, Polina P., Sergey V. Efimov y Vladimir V. Klochkov. "Binding of Different Cyclosporin Variants to Micelles Evidenced by NMR and MD Simulations". Membranes 13, n.º 2 (5 de febrero de 2023): 196. http://dx.doi.org/10.3390/membranes13020196.
Texto completoHuster, Daniel. "Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR". Progress in Nuclear Magnetic Resonance Spectroscopy 46, n.º 2-3 (mayo de 2005): 79–107. http://dx.doi.org/10.1016/j.pnmrs.2005.01.001.
Texto completoTrzepałka, Emilia, Marta Oleszczuk, Maciej Maciejczyk y Bernard Lammek. "Solution structure of conformationally restricted vasopressin analogues." Acta Biochimica Polonica 51, n.º 1 (31 de marzo de 2004): 33–49. http://dx.doi.org/10.18388/abp.2004_3594.
Texto completoYOUNG, Helen, Vikram ROONGTA, Thomas J. DALY y Kevin H. MAYO. "NMR structure and dynamics of monomeric neutrophil-activating peptide 2". Biochemical Journal 338, n.º 3 (8 de marzo de 1999): 591–98. http://dx.doi.org/10.1042/bj3380591.
Texto completoScheidt, Holger A. y Daniel Huster. "Structure and Dynamics of the Myristoyl Lipid Modification of Src Peptides Determined by 2H Solid-State NMR Spectroscopy". Biophysical Journal 96, n.º 9 (mayo de 2009): 3663–72. http://dx.doi.org/10.1016/j.bpj.2009.02.028.
Texto completoBechinger, B. "ChemInform Abstract: The Structure, Dynamics, and Orientation of Antimicrobial Peptides in Membranes by Multidimensional Solid-State NMR Spectroscopy". ChemInform 31, n.º 20 (8 de junio de 2010): no. http://dx.doi.org/10.1002/chin.200020298.
Texto completoWeber, Daniel K. y 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, n.º 3 (2020): 246. http://dx.doi.org/10.1071/ch19307.
Texto completoKaras, John A., David W. Keizer y Marc-Antoine Sani. "Nuclear Magnetic Resonance Study of the Peptide FRANCESSEPAROVIC". Australian Journal of Chemistry 73, n.º 3 (2020): 158. http://dx.doi.org/10.1071/ch19357.
Texto completoSinnaeve, Davy, Abir Ben Bouzayene, Emile Ottoy, Gert-Jan Hofman, Eva Erdmann, Bruno Linclau, Ilya Kuprov, José C. Martins, Vladimir Torbeev y Bruno Kieffer. "Fluorine NMR study of proline-rich sequences using fluoroprolines". Magnetic Resonance 2, n.º 2 (9 de noviembre de 2021): 795–813. http://dx.doi.org/10.5194/mr-2-795-2021.
Texto completoWang, 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, n.º 2 (febrero de 2010): 114–21. http://dx.doi.org/10.1016/j.bbamem.2009.07.028.
Texto completoJacob, Maik H., Roy N. D’Souza, Alexandra I. Lazar y 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, n.º 3 (30 de enero de 2023): 705. http://dx.doi.org/10.3390/polym15030705.
Texto completoŻamojć, Krzysztof, Karolina Streńska, Dariusz Wyrzykowski, Lech Chmurzyński y 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, n.º 10 (23 de septiembre de 2020): 1579. http://dx.doi.org/10.3390/sym12101579.
Texto completoForneris, Federico, B. Tom Burnley y Piet Gros. "Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D". Acta Crystallographica Section D Biological Crystallography 70, n.º 3 (15 de febrero de 2014): 733–43. http://dx.doi.org/10.1107/s1399004713032549.
Texto completoGanicz, Katarzyna. "ChemInform Abstract: Solid State NMR Spectroscopy as a Tool for Investigation of Structure and Dynamics of Amino Acids and Model Peptides". ChemInform 31, n.º 43 (24 de octubre de 2000): no. http://dx.doi.org/10.1002/chin.200043299.
Texto completoFritzsch, Jacob, Alexander Korn, Dayana Surendran, Martin Krueger, Holger A. Scheidt, Kaustubh R. Mote, Perunthiruthy K. Madhu, Sudipta Maiti y Daniel Huster. "Probing the Influence of Single-Site Mutations in the Central Cross-β Region of Amyloid β (1–40) Peptides". Biomolecules 11, n.º 12 (9 de diciembre de 2021): 1848. http://dx.doi.org/10.3390/biom11121848.
Texto completoPatra, Satyajit, Jean-Benoît Claude, Jean-Valère Naubron y Jérome Wenger. "Fast interaction dynamics of G-quadruplex and RGG-rich peptides unveiled in zero-mode waveguides". Nucleic Acids Research 49, n.º 21 (17 de noviembre de 2021): 12348–57. http://dx.doi.org/10.1093/nar/gkab1002.
Texto completoMetcalf, Douglas G., Joseph M. Kielec, Kathleen G. Valentine, A. Joshua Wand, William F. DeGrado y Joel S. Bennett. "NMR Structure of a Disulfide-Crosslinked αIIbβ3 Cytoplasmic Domain Heterodimer". Blood 112, n.º 11 (16 de noviembre de 2008): 2866. http://dx.doi.org/10.1182/blood.v112.11.2866.2866.
Texto completoSzutkowski, Kosma, Emilia Sikorska, Iulia Bakanovych, Amrita Roy Choudhury, Andrej Perdih, Stefan Jurga, Marjana Novič y 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, n.º 17 (26 de agosto de 2019): 4172. http://dx.doi.org/10.3390/ijms20174172.
Texto completoNguyen, Leonard T., Paulus H. S. Kwakman, David I. Chan, Zhihong Liu, Leonie de Boer, Sebastian A. J. Zaat y Hans J. Vogel. "Exploring Platelet Chemokine Antimicrobial Activity: Nuclear Magnetic Resonance Backbone Dynamics of NAP-2 and TC-1". Antimicrobial Agents and Chemotherapy 55, n.º 5 (14 de febrero de 2011): 2074–83. http://dx.doi.org/10.1128/aac.01351-10.
Texto completoZhao, Yue, Songyi Lin, Ruiwen Yang, Dong Chen y Na Sun. "Proton Dynamics of Water Diffusion in Shrimp Hydrolysates Flour and Effects of Moisture Absorption on Its Properties". Foods 10, n.º 5 (20 de mayo de 2021): 1137. http://dx.doi.org/10.3390/foods10051137.
Texto completoSheveleva, Nadezhda N., Irina I. Tarasenko, Mikhail A. Vovk, Mariya E. Mikhailova, Igor M. Neelov y 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, n.º 2 (4 de enero de 2023): 949. http://dx.doi.org/10.3390/ijms24020949.
Texto completoVahidi, Siavash, Zev A. Ripstein, Jordan B. Juravsky, Enrico Rennella, Alfred L. Goldberg, Anthony K. Mittermaier, John L. Rubinstein y 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, n.º 11 (2 de marzo de 2020): 5895–906. http://dx.doi.org/10.1073/pnas.1921630117.
Texto completoWolff, Martin, Klaus Gast, Andreas Evers, Michael Kurz, Stefania Pfeiffer-Marek, Anja Schüler, Robert Seckler y Anja Thalhammer. "A Conserved Hydrophobic Moiety and Helix–Helix Interactions Drive the Self-Assembly of the Incretin Analog Exendin-4". Biomolecules 11, n.º 9 (3 de septiembre de 2021): 1305. http://dx.doi.org/10.3390/biom11091305.
Texto completoNagy, Tamás Milán, Krisztina Knapp, Eszter Illyés, István Timári, Gitta Schlosser, Gabriella Csík, Attila Borics, Zsuzsa Majer y Katalin E. Kövér. "Photochemical and Structural Studies on Cyclic Peptide Models". Molecules 23, n.º 9 (30 de agosto de 2018): 2196. http://dx.doi.org/10.3390/molecules23092196.
Texto completoClemente, Joyce S., Edward G. Gregorich, André J. Simpson, Rajeev Kumar, Denis Courtier-Murias y 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, n.º 1 (2012): 97. http://dx.doi.org/10.1071/en11096.
Texto completoPenk, Anja, Matthias Müller, Holger A. Scheidt, Dieter Langosch y 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, n.º 3 (marzo de 2011): 784–91. http://dx.doi.org/10.1016/j.bbamem.2010.12.015.
Texto completoHenriques, 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, n.º 33 (16 de junio de 2016): 17049–65. http://dx.doi.org/10.1074/jbc.m116.729095.
Texto completovan Well, Renate M., Luciana Marinelli, Cornelis Altona, Kees Erkelens, Gregg Siegal, Mark van Raaij, Antonio L. Llamas-Saiz et al. "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, n.º 36 (septiembre de 2003): 10822–29. http://dx.doi.org/10.1021/ja035461+.
Texto completoArvidsson, Klas, J�ri Jarvet, Peter Allard y 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, n.º 5 (septiembre de 1994): 653–72. http://dx.doi.org/10.1007/bf00404276.
Texto completoMeredith, Jeffrey J., Antoine Dufour y 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, n.º 2 (15 de enero de 2009): 544–51. http://dx.doi.org/10.1021/jp808379x.
Texto completoYee, Adelinda A. y 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, n.º 12 (marzo de 1992): 3135–43. http://dx.doi.org/10.1021/bi00127a014.
Texto completoKokubu, 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, n.º 14 (16 de julio de 2022): 7855. http://dx.doi.org/10.3390/ijms23147855.
Texto completoCharretier, E. y M. Guéron. "Application de la résonance magnétique nucléaire à la détermination de la structure des protéines en solution". Biochemistry and Cell Biology 69, n.º 5-6 (1 de mayo de 1991): 322–35. http://dx.doi.org/10.1139/o91-051.
Texto completoBereiter, Raphael, Maximilian Himmelstoß, Eva Renard, Elisabeth Mairhofer, Michaela Egger, Kathrin Breuker, Christoph Kreutz, Eric Ennifar y Ronald Micura. "Impact of 3-deazapurine nucleobases on RNA properties". Nucleic Acids Research 49, n.º 8 (15 de abril de 2021): 4281–93. http://dx.doi.org/10.1093/nar/gkab256.
Texto completoDeshmukh, Lalit, Rodolfo Ghirlando y 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, n.º 4 (11 de diciembre de 2013): 1043–46. http://dx.doi.org/10.1002/ange.201309127.
Texto completoDeshmukh, Lalit, Rodolfo Ghirlando y 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, n.º 4 (11 de diciembre de 2013): 1025–28. http://dx.doi.org/10.1002/anie.201309127.
Texto completoSgourakis, Nikolaos, Andrew C. McShan, Kannan Natarajan, Vlad K. Kumirov, David Flores-Solis, Jiansheng Jiang, Mareike Badstuebner, Evgenii L. Kovrigin y 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, n.º 1_Supplement (1 de mayo de 2018): 99.23. http://dx.doi.org/10.4049/jimmunol.200.supp.99.23.
Texto completoWang, Jun, Atsushi Tsutsumi, Kiyonobu Yokota, Izuru Kawamura y 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.
Texto completoDeshmukh, Lalit, Rodolfo Ghirlando y 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, n.º 11 (23 de febrero de 2015): 3374–79. http://dx.doi.org/10.1073/pnas.1501985112.
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