Статті в журналах з теми "Conformation Dynamics"
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Ohno, Shiho, Noriyoshi Manabe, Takumi Yamaguchi, Jun Uzawa, and Yoshiki Yamaguchi. "Ribitol in Solution Is an Equilibrium of Asymmetric Conformations." Molecules 26, no. 18 (September 8, 2021): 5471. http://dx.doi.org/10.3390/molecules26185471.
Повний текст джерелаKang, 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 джерелаQu, Kun, Qiuluan Chen, Katarzyna A. Ciazynska, Banghui Liu, Xixi Zhang, Jingjing Wang, Yujie He, et al. "Engineered disulfide reveals structural dynamics of locked SARS-CoV-2 spike." PLOS Pathogens 18, no. 7 (July 29, 2022): e1010583. http://dx.doi.org/10.1371/journal.ppat.1010583.
Повний текст джерелаGuo, Qing, Yufan He, and H. Peter Lu. "Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopy." Proceedings of the National Academy of Sciences 112, no. 45 (October 28, 2015): 13904–9. http://dx.doi.org/10.1073/pnas.1506405112.
Повний текст джерелаLudwiczak, Jan, Ewa Szczęsna, Antônio Marinho da Silva Neto, Piotr Cieplak, Andrzej A. Kasprzak, and Adam Jarmuła. "Interactions between motor domains in kinesin-14 Ncd — a molecular dynamics study." Biochemical Journal 476, no. 17 (September 10, 2019): 2449–62. http://dx.doi.org/10.1042/bcj20190484.
Повний текст джерелаBierzyński, A. "Methods of peptide conformation studies." Acta Biochimica Polonica 48, no. 4 (December 31, 2001): 1091–99. http://dx.doi.org/10.18388/abp.2001_3870.
Повний текст джерелаGaalswyk, Kari, and Christopher N. Rowley. "An explicit-solvent conformation search method using open software." PeerJ 4 (May 31, 2016): e2088. http://dx.doi.org/10.7717/peerj.2088.
Повний текст джерелаLin, Shawn H., Dacheng Zhao, Vivian Deng, Veronica K. Birdsall, Suzanne Ho, Olga Buzovetsky, Candice M. Etson, and Ishita Mukerji. "Integration Host Factor Binds DNA Holliday Junctions." International Journal of Molecular Sciences 24, no. 1 (December 29, 2022): 580. http://dx.doi.org/10.3390/ijms24010580.
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 джерелаVerma, Rajni, Jonathan M. Ellis, and Katie R. Mitchell-Koch. "Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase." Molecules 26, no. 2 (January 7, 2021): 270. http://dx.doi.org/10.3390/molecules26020270.
Повний текст джерелаVerma, Rajni, Jonathan M. Ellis, and Katie R. Mitchell-Koch. "Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase." Molecules 26, no. 2 (January 7, 2021): 270. http://dx.doi.org/10.3390/molecules26020270.
Повний текст джерелаCao, Thong M., and Michael R. King. "Stabilization of the Hinge Region of Human E-selectin Enhances Binding Affinity to Ligands Under Force." Cellular and Molecular Bioengineering 14, no. 1 (February 2021): 65–74. http://dx.doi.org/10.1007/s12195-021-00666-z.
Повний текст джерелаRoh, Soung-Hun, Corey F. Hryc, Hyun-Hwan Jeong, Xue Fei, Joanita Jakana, George H. Lorimer, and Wah Chiu. "Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM." Proceedings of the National Academy of Sciences 114, no. 31 (July 14, 2017): 8259–64. http://dx.doi.org/10.1073/pnas.1704725114.
Повний текст джерелаLane, A. N., T. C. Jenkins, D. J. Brown, and T. Brown. "N.m.r. determination of the solution conformation and dynamics of the A.G mismatch in the d(CGCAAATTGGCG)2 dodecamer." Biochemical Journal 279, no. 1 (October 1, 1991): 269–81. http://dx.doi.org/10.1042/bj2790269.
Повний текст джерелаSavintseva, Liana A., Ilya S. Steshin, Alexander A. Avdoshin, Sergey V. Panteleev, Alexey V. Rozhkov, Ekaterina A. Shirokova, Grigory D. Livshits, et al. "Conformational Dynamics and Stability of Bilayers Formed by Mycolic Acids from the Mycobacterium tuberculosis Outer Membrane." Molecules 28, no. 3 (January 31, 2023): 1347. http://dx.doi.org/10.3390/molecules28031347.
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 джерелаKošovan, Peter, Zuzana Limpouchová, and Karel Procházka. "Charge Distribution and Conformations of Weak Polyelectrolyte Chains in Poor Solvents." Collection of Czechoslovak Chemical Communications 73, no. 4 (2008): 439–58. http://dx.doi.org/10.1135/cccc20080439.
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 джерелаPing, Jie, Pei Hao, Yi-Xue Li, and Jing-Fang Wang. "Molecular Dynamics Studies on the Conformational Transitions of Adenylate Kinase: A Computational Evidence for the Conformational Selection Mechanism." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/628536.
Повний текст джерелаCampbell, Ashley C., Kyle M. Stiers, Julia S. Martin Del Campo, Ritcha Mehra-Chaudhary, Pablo Sobrado, and John J. Tanner. "Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics." Journal of Biological Chemistry 295, no. 38 (July 28, 2020): 13239–49. http://dx.doi.org/10.1074/jbc.ra120.014750.
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 джерелаXu, Xiaojun, Tao Yu, and Shi-Jie Chen. "Understanding the kinetic mechanism of RNA single base pair formation." Proceedings of the National Academy of Sciences 113, no. 1 (December 22, 2015): 116–21. http://dx.doi.org/10.1073/pnas.1517511113.
Повний текст джерелаMIKHAILOV, Dmitri, J. Robert LINHARDT, and H. Kevin MAYO. "NMR solution conformation of heparin-derived hexasaccharide." Biochemical Journal 328, no. 1 (November 15, 1997): 51–61. http://dx.doi.org/10.1042/bj3280051.
Повний текст джерелаAndalib, Payam, Michael J. Wood, and Stephen J. Korn. "Control of Outer Vestibule Dynamics and Current Magnitude in the Kv2.1 Potassium Channel." Journal of General Physiology 120, no. 5 (October 29, 2002): 739–55. http://dx.doi.org/10.1085/jgp.20028639.
Повний текст джерелаAljoundi, Aimen, Ahmed El Rashedy, Patrick Appiah-Kubi та Mahmoud E. S. Soliman. "Coupling of HSP72 α-Helix Subdomains by the Unexpected Irreversible Targeting of Lysine-56 over Cysteine-17; Coevolution of Covalent Bonding". Molecules 25, № 18 (16 вересня 2020): 4239. http://dx.doi.org/10.3390/molecules25184239.
Повний текст джерелаBrenlla, Alfonso, Radoslaw P. Markiewicz, David Rueda, and Louis J. Romano. "Nucleotide selection by the Y-family DNA polymerase Dpo4 involves template translocation and misalignment." Nucleic Acids Research 42, no. 4 (November 21, 2013): 2555–63. http://dx.doi.org/10.1093/nar/gkt1149.
Повний текст джерелаAnselmi, Cecilia, Marisanna Centini, Mirella Scotton, and Alessandro Sega. "Conformation and dynamics in solution of an N-quaternarized benzophenone derivative: a molecule active as UV filter." Canadian Journal of Chemistry 69, no. 6 (June 1, 1991): 913–18. http://dx.doi.org/10.1139/v91-135.
Повний текст джерелаLei, Jiangtao, Xuanyao Li, Mengqiang Cai, Tianjing Guo, Dongdong Lin, Xiaohua Deng, and Yin Li. "Insights into Allosteric Mechanisms of the Lung-Enriched p53 Mutants V157F and R158L." International Journal of Molecular Sciences 23, no. 17 (September 3, 2022): 10100. http://dx.doi.org/10.3390/ijms231710100.
Повний текст джерелаDobrovolska, Olena, Øyvind Strømland, Ørjan Sele Handegård, Martin Jakubec, Morten L. Govasli, Åge Aleksander Skjevik, Nils Åge Frøystein, Knut Teigen, and Øyvind Halskau. "Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles." Molecules 26, no. 12 (June 12, 2021): 3607. http://dx.doi.org/10.3390/molecules26123607.
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 джерелаMIKHAILOV, Dmitri, Kevin H. MAYO, Ioncho R. VLAHOV, Toshihiko TOIDA, Azra PERVIN, and Robert J. LINHARDT. "NMR solution conformation of heparin-derived tetrasaccharide." Biochemical Journal 318, no. 1 (August 15, 1996): 93–102. http://dx.doi.org/10.1042/bj3180093.
Повний текст джерелаZhang, Yiming, Zongzhou Ji, Xin Wang, Yi Cao, and Hai Pan. "Single–Molecule Study of DNAzyme Reveals Its Intrinsic Conformational Dynamics." International Journal of Molecular Sciences 24, no. 2 (January 7, 2023): 1212. http://dx.doi.org/10.3390/ijms24021212.
Повний текст джерелаWu, Si, Liu Hong, Yuqing Wang, Jieqiong Yu, Jie Yang, Jie Yang, Hong Zhang, and Sarah Perrett. "Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function." Proceedings of the National Academy of Sciences 117, no. 14 (March 20, 2020): 7814–23. http://dx.doi.org/10.1073/pnas.1914376117.
Повний текст джерелаMahboub, Radia. "Dynamics Simulation Studies of Solvation Effect on the Trans-Xylomollin Conformation." International Letters of Chemistry, Physics and Astronomy 13 (September 2013): 132–46. http://dx.doi.org/10.18052/www.scipress.com/ilcpa.13.132.
Повний текст джерелаMahboub, Radia. "Dynamics Simulation Studies of Solvation Effect on the Trans-Xylomollin Conformation." International Letters of Chemistry, Physics and Astronomy 13 (May 3, 2013): 132–46. http://dx.doi.org/10.56431/p-694v14.
Повний текст джерелаBennett, Ashley Lauren, and Rory Henderson. "HIV-1 Envelope Conformation, Allostery, and Dynamics." Viruses 13, no. 5 (May 7, 2021): 852. http://dx.doi.org/10.3390/v13050852.
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 джерелаPasenkiewicz-Gierula, M., and T. Róg. "Conformations, orientations and time scales characterising dimyristoylphosphatidylcholine bilayer membrane. Molecular dynamics simulation studies." Acta Biochimica Polonica 44, no. 3 (September 30, 1997): 607–24. http://dx.doi.org/10.18388/abp.1997_4409.
Повний текст джерелаChen, Hui, Daniel M. Cohen, Dilshad M. Choudhury, Noriyuki Kioka, and Susan W. Craig. "Spatial distribution and functional significance of activated vinculin in living cells." Journal of Cell Biology 169, no. 3 (May 9, 2005): 459–70. http://dx.doi.org/10.1083/jcb.200410100.
Повний текст джерелаPaz, Aviv, Derek P. Claxton, Jay Prakash Kumar, Kelli Kazmier, Paola Bisignano, Shruti Sharma, Shannon A. Nolte, et al. "Conformational transitions of the sodium-dependent sugar transporter, vSGLT." Proceedings of the National Academy of Sciences 115, no. 12 (March 5, 2018): E2742—E2751. http://dx.doi.org/10.1073/pnas.1718451115.
Повний текст джерелаChen, Baohua, Sujit Basak, Peng Chen, Changcheng Zhang, Kay Perry, Songhai Tian, Clinton Yu, et al. "Structure and conformational dynamics of Clostridioides difficile toxin A." Life Science Alliance 5, no. 6 (March 15, 2022): e202201383. http://dx.doi.org/10.26508/lsa.202201383.
Повний текст джерелаDubovskii, Peter V., Kira M. Dubova, Gleb Bourenkov, Vladislav G. Starkov, Anastasia G. Konshina, Roman G. Efremov, Yuri N. Utkin, and Valeriya R. Samygina. "Variability in the Spatial Structure of the Central Loop in Cobra Cytotoxins Revealed by X-ray Analysis and Molecular Modeling." Toxins 14, no. 2 (February 18, 2022): 149. http://dx.doi.org/10.3390/toxins14020149.
Повний текст джерелаNinaber, Alex, and J. M. Goodfellow. "DNA conformation and dynamics." Radiation and Environmental Biophysics 38, no. 1 (May 12, 1999): 23–29. http://dx.doi.org/10.1007/s004110050134.
Повний текст джерелаLuo, Liaofu. "Conformation dynamics of macromolecules." International Journal of Quantum Chemistry 32, no. 4 (October 1987): 435–50. http://dx.doi.org/10.1002/qua.560320404.
Повний текст джерелаBuckley, David P., Marie E. Migaud, and John J. Tanner. "Conformational Preferences of Pyridone Adenine Dinucleotides from Molecular Dynamics Simulations." International Journal of Molecular Sciences 23, no. 19 (October 6, 2022): 11866. http://dx.doi.org/10.3390/ijms231911866.
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 джерелаSamsonov, Sergey A., Stephan Theisgen, Thomas Riemer, Daniel Huster, and M. Teresa Pisabarro. "Glycosaminoglycan Monosaccharide Blocks Analysis by Quantum Mechanics, Molecular Dynamics, and Nuclear Magnetic Resonance." BioMed Research International 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/808071.
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 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 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.
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