Статті в журналах з теми "Proteins - Conformation Dynamics"
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Kang, Hyun-Seo, and Michael Sattler. "Capturing dynamic conformational shifts in protein–ligand recognition using integrative structural biology in solution." Emerging Topics in Life Sciences 2, no. 1 (April 20, 2018): 107–19. http://dx.doi.org/10.1042/etls20170090.
Повний текст джерелаGaraizar, Adiran, Ignacio Sanchez-Burgos, Rosana Collepardo-Guevara, and Jorge R. Espinosa. "Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid–Liquid Phase Separation." Molecules 25, no. 20 (October 15, 2020): 4705. http://dx.doi.org/10.3390/molecules25204705.
Повний текст джерелаBrouhard, Gary J., та Luke M. Rice. "The contribution of αβ-tubulin curvature to microtubule dynamics". Journal of Cell Biology 207, № 3 (10 листопада 2014): 323–34. http://dx.doi.org/10.1083/jcb.201407095.
Повний текст джерелаGormal, Rachel S., Pranesh Padmanabhan, Ravikiran Kasula, Adekunle T. Bademosi, Sean Coakley, Jean Giacomotto, Ailisa Blum та ін. "Modular transient nanoclustering of activated β2-adrenergic receptors revealed by single-molecule tracking of conformation-specific nanobodies". Proceedings of the National Academy of Sciences 117, № 48 (19 листопада 2020): 30476–87. http://dx.doi.org/10.1073/pnas.2007443117.
Повний текст джерелаMizutani, Tadashi, and Shigeyuki Yagi. "Linear tetrapyrroles as functional pigments in chemistry and biology." Journal of Porphyrins and Phthalocyanines 08, no. 03 (March 2004): 226–37. http://dx.doi.org/10.1142/s1088424604000210.
Повний текст джерелаRamirez-Mondragon, Carlos A., Megin E. Nguyen, Jozafina Milicaj, Bakar A. Hassan, Frank J. Tucci, Ramaiah Muthyala, Jiali Gao, Erika A. Taylor, and Yuk Y. Sham. "Conserved Conformational Hierarchy across Functionally Divergent Glycosyltransferases of the GT-B Structural Superfamily as Determined from Microsecond Molecular Dynamics." International Journal of Molecular Sciences 22, no. 9 (April 28, 2021): 4619. http://dx.doi.org/10.3390/ijms22094619.
Повний текст джерелаKulkarni, Prakash, Vitor B. P. Leite, Susmita Roy, Supriyo Bhattacharyya, Atish Mohanty, Srisairam Achuthan, Divyoj Singh, et al. "Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma." Biophysics Reviews 3, no. 1 (March 2022): 011306. http://dx.doi.org/10.1063/5.0080512.
Повний текст джерелаWestenhoff, Sebastian, Elena Nazarenko, Erik Malmerberg, Jan Davidsson, Gergely Katona, and Richard Neutze. "Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches." Acta Crystallographica Section A Foundations of Crystallography 66, no. 2 (February 18, 2010): 207–19. http://dx.doi.org/10.1107/s0108767309054361.
Повний текст джерелаYang, Jing, Jing Chen, and Zibiao Li. "Structural Basis for the Structure–Activity Behaviour of Oxaliplatin and its Enantiomeric Analogues: A Molecular Dynamics Study of Platinum-DNA Intrastrand Crosslink Adducts." Australian Journal of Chemistry 69, no. 4 (2016): 379. http://dx.doi.org/10.1071/ch15624.
Повний текст джерелаLi, Haiyan, Zanxia Cao, Guodong Hu, Liling Zhao, Chunling Wang, and Jihua Wang. "Ligand-induced structural changes analysis of ribose-binding protein as studied by molecular dynamics simulations." Technology and Health Care 29 (March 25, 2021): 103–14. http://dx.doi.org/10.3233/thc-218011.
Повний текст джерелаNehls, Thomas, Tim Heymann, Christian Meyners, Felix Hausch, and Frederik Lermyte. "Fenton-Chemistry-Based Oxidative Modification of Proteins Reflects Their Conformation." International Journal of Molecular Sciences 22, no. 18 (September 14, 2021): 9927. http://dx.doi.org/10.3390/ijms22189927.
Повний текст джерелаLenaz, Giorgio. "Lipid fluidity and membrane protein dynamics." Bioscience Reports 7, no. 11 (November 1, 1987): 823–37. http://dx.doi.org/10.1007/bf01119473.
Повний текст джерелаEvich, Marina, Alexander M. Spring-Connell, and Markus W. Germann. "Impact of modified ribose sugars on nucleic acid conformation and function." Heterocyclic Communications 23, no. 3 (June 27, 2017): 155–65. http://dx.doi.org/10.1515/hc-2017-0056.
Повний текст джерелаZhong, Bozitao, Ge Song, and Hai-Feng Chen. "Balanced Force Field ff03CMAP Improving the Dynamics Conformation Sampling of Phosphorylation Site." International Journal of Molecular Sciences 23, no. 19 (September 25, 2022): 11285. http://dx.doi.org/10.3390/ijms231911285.
Повний текст джерелаZhang, Meiling, Thomas E. Frederick, Jamie VanPelt, David A. Case, and Jeffrey W. Peng. "Coupled intra- and interdomain dynamics support domain cross-talk in Pin1." Journal of Biological Chemistry 295, no. 49 (September 22, 2020): 16585–603. http://dx.doi.org/10.1074/jbc.ra120.015849.
Повний текст джерелаRoither, Bernhard, Chris Oostenbrink, Georg Pfeiler, Heinz Koelbl, and Wolfgang Schreiner. "Pembrolizumab Induces an Unexpected Conformational Change in the CC′-loop of PD-1." Cancers 13, no. 1 (December 22, 2020): 5. http://dx.doi.org/10.3390/cancers13010005.
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 джерелаDay, Austin L., Per Greisen, Lindsey Doyle, Alberto Schena, Nephi Stella, Kai Johnsson, David Baker, and Barry Stoddard. "Unintended specificity of an engineered ligand-binding protein facilitated by unpredicted plasticity of the protein fold." Protein Engineering, Design and Selection 31, no. 10 (October 1, 2018): 375–87. http://dx.doi.org/10.1093/protein/gzy031.
Повний текст джерелаKim, J. I., K. Eom, and S. Na. "Mechanical Mass-Spring Model for Understanding Globular Motion of Proteins." Journal of Mechanics 32, no. 2 (January 25, 2016): 123–29. http://dx.doi.org/10.1017/jmech.2015.109.
Повний текст джерелаLaugwitz, Jeannette M., Haleh H. Haeri, Anette Kaiser, Ulrike Krug, Dariush Hinderberger, Annette G. Beck-Sickinger, and Peter Schmidt. "Probing the Y2 Receptor on Transmembrane, Intra- and Extra-Cellular Sites for EPR Measurements." Molecules 25, no. 18 (September 10, 2020): 4143. http://dx.doi.org/10.3390/molecules25184143.
Повний текст джерелаSharma, Meenakshi, Nancy Jaiswal, Dinesh Kumar, and Krishna Mohan Poluri. "Enhanced dynamics of conformationally heterogeneous T7 bacteriophage lysozyme native state attenuates its stability and activity." Biochemical Journal 476, no. 3 (February 14, 2019): 613–28. http://dx.doi.org/10.1042/bcj20180703.
Повний текст джерелаPistolesi, Sara, Nico Tjandra, and Guillermo A. Bermejo. "Solution NMR studies of periplasmic binding proteins and their interaction partners." BioMolecular Concepts 2, no. 1-2 (April 1, 2011): 53–64. http://dx.doi.org/10.1515/bmc.2011.005.
Повний текст джерелаTafi, A., Fabrizio Manetti, Federico Corelli, Stefano Alcaro, and Maurizio Botta. "Structural flexibility of hyaluronan oligomers as probed by molecular modelling." Pure and Applied Chemistry 75, no. 2-3 (January 1, 2003): 359–66. http://dx.doi.org/10.1351/pac200375020359.
Повний текст джерелаKrukenberg, Kristin A., Timothy O. Street, Laura A. Lavery, and David A. Agard. "Conformational dynamics of the molecular chaperone Hsp90." Quarterly Reviews of Biophysics 44, no. 2 (March 18, 2011): 229–55. http://dx.doi.org/10.1017/s0033583510000314.
Повний текст джерелаTamrazi, Anobel, Kathryn E. Carlson, Alice L. Rodriguez, and John A. Katzenellenbogen. "Coactivator Proteins as Determinants of Estrogen Receptor Structure and Function: Spectroscopic Evidence for a Novel Coactivator-Stabilized Receptor Conformation." Molecular Endocrinology 19, no. 6 (June 1, 2005): 1516–28. http://dx.doi.org/10.1210/me.2004-0458.
Повний текст джерелаSun, Jixue, Zibin Li, and Na Yang. "Mechanism of the Conformational Change of the Protein Methyltransferase SMYD3: A Molecular Dynamics Simulation Study." International Journal of Molecular Sciences 22, no. 13 (July 2, 2021): 7185. http://dx.doi.org/10.3390/ijms22137185.
Повний текст джерелаVollmer, B., V. Pražák, D. Vasishtan, E. E. Jefferys, A. Hernandez-Duran, M. Vallbracht, B. G. Klupp, et al. "The prefusion structure of herpes simplex virus glycoprotein B." Science Advances 6, no. 39 (September 2020): eabc1726. http://dx.doi.org/10.1126/sciadv.abc1726.
Повний текст джерелаCaldararu, Octav, Vilhelm Ekberg, Derek T. Logan, Esko Oksanen, and Ulf Ryde. "Exploring ligand dynamics in protein crystal structures with ensemble refinement." Acta Crystallographica Section D Structural Biology 77, no. 8 (July 29, 2021): 1099–115. http://dx.doi.org/10.1107/s2059798321006513.
Повний текст джерелаLIEBOVITCH, LARRY S., NIKITA D. ARNOLD, and LEV Y. SELECTOR. "NEURAL NETWORKS TO COMPUTE MOLECULAR DYNAMICS." Journal of Biological Systems 02, no. 02 (June 1994): 193–228. http://dx.doi.org/10.1142/s0218339094000155.
Повний текст джерелаRen, Zhenning, Jumin Lee, Mahdi Muhammad Moosa, Yin Nian, Liya Hu, Zhichun Xu, Jason G. McCoy, Allan Chris M. Ferreon, Wonpil Im, and Ming Zhou. "Structure of an EIIC sugar transporter trapped in an inward-facing conformation." Proceedings of the National Academy of Sciences 115, no. 23 (May 21, 2018): 5962–67. http://dx.doi.org/10.1073/pnas.1800647115.
Повний текст джерелаStewart, Chelsea M., Cosmo Z. Buffalo, J. Andrés Valderrama, Anna Henningham, Jason N. Cole, Victor Nizet, and Partho Ghosh. "Coiled-coil destabilizing residues in the group A Streptococcus M1 protein are required for functional interaction." Proceedings of the National Academy of Sciences 113, no. 34 (August 10, 2016): 9515–20. http://dx.doi.org/10.1073/pnas.1606160113.
Повний текст джерелаLi, Qingxin, and CongBao Kang. "Insights into Structures and Dynamics of Flavivirus Proteases from NMR Studies." International Journal of Molecular Sciences 21, no. 7 (April 5, 2020): 2527. http://dx.doi.org/10.3390/ijms21072527.
Повний текст джерелаFidy, Judit, Monique Laberge, Beata Ullrich, Laszlo Polgar, Zoltan Szeltner, Jacques Gallay, and Michel Vincent. "Tryptophan rotamers that report the conformational dynamics of proteins." Pure and Applied Chemistry 73, no. 3 (January 1, 2001): 415–19. http://dx.doi.org/10.1351/pac200173030415.
Повний текст джерелаRief, Matthias, Filipp Oesterhelt, Hauke Clausen-Schaumann, and Hermann E. Gaub. "Structural Forces in Biomolecules." Microscopy and Microanalysis 5, S2 (August 1999): 1016–17. http://dx.doi.org/10.1017/s1431927600018407.
Повний текст джерелаCamacho, Inês S., Alina Theisen, Linus O. Johannissen, L. Aranzazú Díaz-Ramos, John M. Christie, Gareth I. Jenkins, Bruno Bellina, Perdita Barran, and Alex R. Jones. "Native mass spectrometry reveals the conformational diversity of the UVR8 photoreceptor." Proceedings of the National Academy of Sciences 116, no. 4 (January 4, 2019): 1116–25. http://dx.doi.org/10.1073/pnas.1813254116.
Повний текст джерелаLangan, Patricia S., Venu Gopal Vandavasi, Wojciech Kopec, Brendan Sullivan, Pavel V. Afonne, Kevin L. Weiss, Bert L. de Groot, and Leighton Coates. "The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation." IUCrJ 7, no. 5 (July 25, 2020): 835–43. http://dx.doi.org/10.1107/s2052252520008271.
Повний текст джерелаWen, Lai, Alex Marki, Payel Roy, Sara McArdle, Hao Sun, Zhichao Fan, Alexandre R. Gingras, Mark H. Ginsberg та Klaus Ley. "Recruitment of kindlin-3 to plasma membrane through its PH domain precedes high affinity β2 integrin activation and neutrophil arrest". Journal of Immunology 204, № 1_Supplement (1 травня 2020): 220.7. http://dx.doi.org/10.4049/jimmunol.204.supp.220.7.
Повний текст джерелаTyagi, Vivek, Victor Vasquez-Montes, J. Alfredo Freites, Alexander Kyrychenko, Douglas J. Tobias, and Alexey S. Ladokhin. "Effects of Cardiolipin on the Conformational Dynamics of Membrane-Anchored Bcl-xL." International Journal of Molecular Sciences 22, no. 17 (August 30, 2021): 9388. http://dx.doi.org/10.3390/ijms22179388.
Повний текст джерелаCraggs, Timothy D., Marko Sustarsic, Anne Plochowietz, Majid Mosayebi, Hendrik Kaju, Andrew Cuthbert, Johannes Hohlbein, et al. "Substrate conformational dynamics facilitate structure-specific recognition of gapped DNA by DNA polymerase." Nucleic Acids Research 47, no. 20 (September 23, 2019): 10788–800. http://dx.doi.org/10.1093/nar/gkz797.
Повний текст джерелаBeier, David H., Tucker J. Carrocci, Clarisse van der Feltz, U. Sandy Tretbar, Joshua C. Paulson, Nikolai Grabowski, and Aaron A. Hoskins. "Dynamics of the DEAD-box ATPase Prp5 RecA-like domains provide a conformational switch during spliceosome assembly." Nucleic Acids Research 47, no. 20 (September 6, 2019): 10842–51. http://dx.doi.org/10.1093/nar/gkz765.
Повний текст джерелаTarjányi, Tamás, Ferenc Bogár, Janos Minarovits, Márió Gajdács, and Zsolt Tóth. "Interaction of KRSR Peptide with Titanium Dioxide Anatase (100) Surface: A Molecular Dynamics Simulation Study." International Journal of Molecular Sciences 22, no. 24 (December 9, 2021): 13251. http://dx.doi.org/10.3390/ijms222413251.
Повний текст джерелаGoricanec, David, Ralf Stehle, Pascal Egloff, Simina Grigoriu, Andreas Plückthun, Gerhard Wagner та Franz Hagn. "Conformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding". Proceedings of the National Academy of Sciences 113, № 26 (13 червня 2016): E3629—E3638. http://dx.doi.org/10.1073/pnas.1604125113.
Повний текст джерелаMott, Helen R., and Darerca Owen. "Allostery and dynamics in small G proteins." Biochemical Society Transactions 46, no. 5 (October 9, 2018): 1333–43. http://dx.doi.org/10.1042/bst20170569.
Повний текст джерелаHu, Gang, Jiye Fu, Yi Qiao, Hao Meng, Zunliang Wang, Jing Tu, and Zuhong Lu. "Molecular dynamics discrimination of the conformational states of calmodulin through solid-state nanopores." Physical Chemistry Chemical Physics 22, no. 34 (2020): 19188–94. http://dx.doi.org/10.1039/d0cp02500c.
Повний текст джерелаLakomek, Nils-Alexander, Halenur Yavuz, Reinhard Jahn, and Ángel Pérez-Lara. "Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion." Proceedings of the National Academy of Sciences 116, no. 18 (April 11, 2019): 8699–708. http://dx.doi.org/10.1073/pnas.1813194116.
Повний текст джерелаMartini, Silvia, Claudia Bonechi, Alberto Foletti, and Claudio Rossi. "Water-Protein Interactions: The Secret of Protein Dynamics." Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/138916.
Повний текст джерелаDas, Ananya, Nichole Adiletta, and Dmitri N. Ermolenko. "Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases." International Journal of Molecular Sciences 24, no. 8 (April 7, 2023): 6878. http://dx.doi.org/10.3390/ijms24086878.
Повний текст джерелаBiedermannová, Lada, and Bohdan Schneider. "Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 27, 2015): 2192–202. http://dx.doi.org/10.1107/s1399004715015679.
Повний текст джерелаGiampà, Marco, and Elvira Sgobba. "Insight to Functional Conformation and Noncovalent Interactions of Protein-Protein Assembly Using MALDI Mass Spectrometry." Molecules 25, no. 21 (October 28, 2020): 4979. http://dx.doi.org/10.3390/molecules25214979.
Повний текст джерелаDevlin, Jason, Jesus Alonso, Grant Keller, Sara Bobisse, Alexandre Harari, and Brian Baker. "4094 Structural Determinants of Immunogenicity for Peptide-Based Immunotherapy." Journal of Clinical and Translational Science 4, s1 (June 2020): 16. http://dx.doi.org/10.1017/cts.2020.92.
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