Literatura académica sobre el tema "Proteins - Conformation Dynamics"
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Artículos de revistas sobre el tema "Proteins - Conformation Dynamics"
Kang, Hyun-Seo y Michael Sattler. "Capturing dynamic conformational shifts in protein–ligand recognition using integrative structural biology in solution". Emerging Topics in Life Sciences 2, n.º 1 (20 de abril de 2018): 107–19. http://dx.doi.org/10.1042/etls20170090.
Texto completoGaraizar, Adiran, Ignacio Sanchez-Burgos, Rosana Collepardo-Guevara y Jorge R. Espinosa. "Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid–Liquid Phase Separation". Molecules 25, n.º 20 (15 de octubre de 2020): 4705. http://dx.doi.org/10.3390/molecules25204705.
Texto completoBrouhard, Gary J. y Luke M. Rice. "The contribution of αβ-tubulin curvature to microtubule dynamics". Journal of Cell Biology 207, n.º 3 (10 de noviembre de 2014): 323–34. http://dx.doi.org/10.1083/jcb.201407095.
Texto completoGormal, Rachel S., Pranesh Padmanabhan, Ravikiran Kasula, Adekunle T. Bademosi, Sean Coakley, Jean Giacomotto, Ailisa Blum et al. "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, n.º 48 (19 de noviembre de 2020): 30476–87. http://dx.doi.org/10.1073/pnas.2007443117.
Texto completoMizutani, Tadashi y Shigeyuki Yagi. "Linear tetrapyrroles as functional pigments in chemistry and biology". Journal of Porphyrins and Phthalocyanines 08, n.º 03 (marzo de 2004): 226–37. http://dx.doi.org/10.1142/s1088424604000210.
Texto completoRamirez-Mondragon, Carlos A., Megin E. Nguyen, Jozafina Milicaj, Bakar A. Hassan, Frank J. Tucci, Ramaiah Muthyala, Jiali Gao, Erika A. Taylor y 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, n.º 9 (28 de abril de 2021): 4619. http://dx.doi.org/10.3390/ijms22094619.
Texto completoKulkarni, 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, n.º 1 (marzo de 2022): 011306. http://dx.doi.org/10.1063/5.0080512.
Texto completoWestenhoff, Sebastian, Elena Nazarenko, Erik Malmerberg, Jan Davidsson, Gergely Katona y Richard Neutze. "Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches". Acta Crystallographica Section A Foundations of Crystallography 66, n.º 2 (18 de febrero de 2010): 207–19. http://dx.doi.org/10.1107/s0108767309054361.
Texto completoYang, Jing, Jing Chen y 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, n.º 4 (2016): 379. http://dx.doi.org/10.1071/ch15624.
Texto completoLi, Haiyan, Zanxia Cao, Guodong Hu, Liling Zhao, Chunling Wang y Jihua Wang. "Ligand-induced structural changes analysis of ribose-binding protein as studied by molecular dynamics simulations". Technology and Health Care 29 (25 de marzo de 2021): 103–14. http://dx.doi.org/10.3233/thc-218011.
Texto completoTesis sobre el tema "Proteins - Conformation Dynamics"
Ceres, Nicoletta. "Coarse-grain modeling of proteins : mechanics, dynamics and function". Thesis, Lyon 1, 2012. http://www.theses.fr/2012LYO10030.
Texto completoProteins are flexible molecules, which accomplish a variety of cellular tasks through mechanical motions and conformational fluctuations encoded in their three-dimensional structure. Amongst the theoretical approaches contributing to a better understanding of the relationship between protein structure, mechanics, dynamics and function, coarse-grain models are a powerful tool. They can be used to integrate structural and dynamic information over broad time and size scales at a low computational cost, achieved by averaging out the less important degrees of freedom. In this work, fast comparative studies of protein flexibility and mechanics have been performed with the simple coarse-grain Elastic Network Model. However, the dependency of the results on the starting conformation, and the rather constrained backbone dynamics imposed by the harmonic approximation, motivated the development of a new approach, for a more extensive exploration of conformational space. These efforts led to the PaLaCe model, designed to allow significant changes in secondary structure, while maintaining residue specificity despite a lower-level resolution. Using PaLaCe, we were able to reproduce two processes involving protein plasticity: the mechanical unfolding of the I27 domain of the giant muscle protein titin and the near-native dynamics of two homologous enzymes adapted to work at different temperatures. Agreement with experimental data and results from published atomistic models demonstrate that PaLaCe is a reliable, sufficiently accurate, but computationally inexpensive approach. It therefore opens the doors for a systematic investigation of the link between protein dynamics/mechanics and function
Kragelj, Jaka. "Structure and dynamics of intrinsically disordered regions of MAPK signalling proteins". Thesis, Grenoble, 2014. http://www.theses.fr/2014GRENV060/document.
Texto completoProtein signal transduction pathways allow cells respond to and process signals from the environment. A group of such pathways, called mitogen-activated protein kinase (MAPK) signal transduction pathways, is well conserved in all eukaryotic cells and is involved in regulating many important cell processes. Long intrinsically disordered region (IDRs), present in many MAPKs, have remained structurally uncharacterised. The IDRs of MAPKs are especially important as they contain docking-site motifs which control the interactions between MAPK proteins themselves and also between MAPKs and other interacting proteins containing the same motifs. Nuclear magnetic resonance (NMR) spectroscopy in combination with other biophysical techniques was used to study IDRs of MAPKs. NMR spectroscopy is well suited for studying intrinsically disordered proteins (IDPs) at atomic-level resolution. NMR observables, such as for example chemical shifts and residual dipolar couplings, can be used together with ensemble selection methods to study residual structure in IDRs. Nuclear spin relaxation informs us about fast pico-nanosecond motions. NMR titrations and exchange spectroscopy techniques can be used to monitor kinetics of protein-protein interactions. The mechanistic insight into function of IDRs and motifs will contribute to understanding of how signal transduction pathways work
Murzycki, Jennifer E. "Probing Protein Dynamics Through Mutational and Computational Studies of HIV-1 Protease: A Dissertation". eScholarship@UMMS, 2006. https://escholarship.umassmed.edu/gsbs_diss/166.
Texto completoAbyzov, Anton. "Nuclear Magnetic Resonance Studies of the Dynamics and Thermodynamics of Intrinsically Disordered Proteins". Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAY026/document.
Texto completoIntrinsically disordered proteins (IDPs) are highly flexible heteropolymers, implicated in important cellular activities (signal transduction, molecular recognition, transcription, translation, etc.) and representing potential drug targets against cancer and neurodegenerative diseases, whose dynamic modes define their biological function. Although the conformational states sampled by IDPs are relatively well understood, essentially nothing is known about the associated dynamic timescales. In this study we investigate the conformational behavior of the intrinsically disordered C-terminal domain of the nucleoprotein of Sendai virus (NTAIL), which interacts with the PX domain of the phosphoprotein. The interaction site has been shown to sample an equilibrium of discrete helices in the free state, which forms an encounter complex implicating the stabilization of one of the helical conformers upon interaction with PX, prior to diffusing on the surface of PX and engaging in the actual binding site. However, very little is known about the timescales of chain motions, which surely play a role in the interaction kinetics, in particular in terms of the on-rate of the interaction. This 124 amino acid protein also provides a good model system, containing long unfolded domains with chain-like dynamics and regions with residual structure. The measurement of extensive set of coherent relaxation rates at multiple magnetic fields, multiple temperatures and in three different length constructs of the same IDP has allowed us to characterize the dynamic nature of NTAIL in unprecedented detail. By analyzing the relaxation data using extended model-free approach, we show that fast (≤ 50 ps) components of the correlation function report on librational motions. A dominant mode occurs on timescales around one nanosecond, apparently reporting on backbone sampling within Ramachandran sub-states, while a slower component (5-25 ns) reports on segmental dynamics dominated by the chain-like nature of the protein. The ability to delineate intrinsic modes and timescales will improve our understanding of the behavior and function of IDPs
Link, Justin J. "Ultrafast Protein Conformation Dynamics". The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1230584570.
Texto completoDorywalska, Magdalena. "Conformational dynamics of protein synthesis /". May be available electronically:, 2007. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.
Texto completoZang, Chen. "Ultrafast Spectroscopic Study of Protein Conformation Dynamics and Hydration Dynamics". The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1299481658.
Texto completoBossa, Cecilia. "Conformational fluctuations in proteins. A molecular dynamics based study". Doctoral thesis, La Sapienza, 2005. http://hdl.handle.net/11573/916821.
Texto completoChen, Wei. "Molecular dynamics simulations of binding, unfolding, and global conformational changes of signaling and adhesion molecules". Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/28118.
Texto completoCommittee Chair: Zhu, Cheng; Committee Member: Harvey, Stephen; Committee Member: Hud, Nicholas; Committee Member: Zamir, Evan; Committee Member: Zhu, Ting.
Bruce, Neil John. "Investigating protein conformational change via molecular dynamics simulation". Thesis, University of Manchester, 2011. https://www.research.manchester.ac.uk/portal/en/theses/investigating-protein-conformational-change-via-molecular-dynamics-simulation(17145939-f643-4b23-bbb9-029cf5489c15).html.
Texto completoLibros sobre el tema "Proteins - Conformation Dynamics"
Livesay, Dennis R. Protein dynamics: Methods and protocols. New York: Humana Press, 2013.
Buscar texto completoSubbiah, S. Protein motions. New York: Chaoman & Hall, 1996.
Buscar texto completoInternational Symposium on Structure and Dynamics of Nucleic Acids, Proteins, and Membranes (1986 Riva, Italy). Structure and dynamics of nucleic acids, proteins, and membranes. New York: Plenum Press, 1986.
Buscar texto completoHan, Ke-li, Xin Zhang y Ming-jun Yang, eds. Protein Conformational Dynamics. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-02970-2.
Texto completoRupp, Bernhard. Biomolecular crystallography. New York, NY: Garland Science, 2010.
Buscar texto completoRupp, Bernhard. Biomolecular crystallography. New York, NY: Garland Science, 2010.
Buscar texto completoCourse on Dynamics and the Problem of Recognition in Biological Macromolecules (2nd 1995 Erice, Italy). Dynamics and the problem of recognition in biological macromolecules. New York: Plenum Press, 1996.
Buscar texto completoXin, Zhang, Ke-li Han y Ming-jun Yang. Protein Conformational Dynamics. Springer, 2014.
Buscar texto completoXin, Zhang, Ke-Li Han y Ming-jun Yang. Protein Conformational Dynamics. Springer International Publishing AG, 2016.
Buscar texto completoXin, Zhang, Ke-Li Han y Ming-jun Yang. Protein Conformational Dynamics. Springer London, Limited, 2014.
Buscar texto completoCapítulos de libros sobre el tema "Proteins - Conformation Dynamics"
Balasubramaniam, A., S. G. Huang, S. Sheriff, M. Prabhakaran y V. Renugopalakrishnan. "Solution conformation of neuropeptide Y: 2D NMR and molecular dynamics studies". En Proteins, 79–81. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_11.
Texto completoWüthrich, Kurt. "Conformation of Non-Crystalline Proteins Viewed by NMR". En Structure and Dynamics of Nucleic Acids, Proteins, and Membranes, 21–29. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5308-9_2.
Texto completoChoi, Ucheor B., Keith R. Weninger y Mark E. Bowen. "Immobilization of Proteins for Single-Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and Dynamics". En Intrinsically Disordered Protein Analysis, 3–20. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3704-8_1.
Texto completoSo, Pui-Kin. "Hydrogen–Deuterium Exchange Mass Spectrometry for Probing Changes in Conformation and Dynamics of Proteins". En Methods in Molecular Biology, 159–73. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0892-0_10.
Texto completoMao, Youdong. "Structure, Dynamics and Function of the 26S Proteasome". En Subcellular Biochemistry, 1–151. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-58971-4_1.
Texto completoBarth, Marie y Carla Schmidt. "Quantitative Cross-Linking of Proteins and Protein". En Methods in Molecular Biology, 385–400. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1024-4_26.
Texto completoTan, Yan-Wen, Jeffrey A. Hanson, Jhih-Wei Chu y Haw Yang. "Confocal Single-Molecule FRET for Protein Conformational Dynamics". En Protein Dynamics, 51–62. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-658-0_3.
Texto completoZheng, Wenjun y Mustafa Tekpinar. "Analysis of Protein Conformational Transitions Using Elastic Network Model". En Protein Dynamics, 159–72. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-658-0_9.
Texto completoEichinger, Markus, Berthold Heymann, Helmut Heller, Helmut Grubmüller y Paul Tavan. "Conformational Dynamics Simulations of Proteins". En Computational Molecular Dynamics: Challenges, Methods, Ideas, 78–97. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-58360-5_4.
Texto completoHills, Ronald D. "Balancing Bond, Nonbond, and Gō-Like Terms in Coarse Grain Simulations of Conformational Dynamics". En Protein Dynamics, 123–40. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-658-0_7.
Texto completoActas de conferencias sobre el tema "Proteins - Conformation Dynamics"
Karplus, M. "Internal dynamics of macromolecules : Simulations of motion in proteins". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.thb1.
Texto completoXu, Yangqing y Gang Bao. "Protein Conformational Changes Under Applied Forces". En ASME 1999 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1999. http://dx.doi.org/10.1115/imece1999-0408.
Texto completoKazerounian, Kazem, Khalid Latif, Kimberly Rodriguez y Carlos Alvarado. "ProtoFold: Part I — Nanokinematics for Analysis of Protein Molecules". En ASME 2004 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/detc2004-57243.
Texto completoDyer, R. Brian y Timothy P. Causgrove. "Ultrafast Protein Relaxation: Time-Resolved Infrared Studies of Protein Dynamics Triggered by CO Photodissociation from CO Myoglobin". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/up.1994.tub.4.
Texto completoLim, Manko, Timothy A. Jackson y Philip A. Anfinrud. "Ultrafast Near-IR Spectroscopy of Carbonmonoxymyoglobin: the Dynamics of Protein Relaxation". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.thb3.
Texto completoJewel, Yead, Prashanta Dutta y Jin Liu. "Coarse-Grained Molecular Dynamics Simulations of Sugar Transport Across Lactose Permease". En ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52337.
Texto completoLeeson, D. Thorn y D. A. Wiersma. "Long-Lived Stimulated Photon Echo Studies of Protein and Glass Dynamics". En Spectral Hole-Burning and Related Spectroscopies: Science and Applications. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/shbs.1994.thb1.
Texto completoMaghsoodi, Ameneh, Anupam Chatterjee, Ioan Andricioaei y Noel Perkins. "An Approximate Model of the Dynamics of the Bacteriophage T4 Injection Machinery". En ASME 2016 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2016. http://dx.doi.org/10.1115/detc2016-60281.
Texto completoCortés, Juan y Ibrahim Al-Bluwi. "A Robotics Approach to Enhance Conformational Sampling of Proteins". En ASME 2012 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/detc2012-70105.
Texto completoBao, Gang y Shannon Stott. "Langevin Dynamics of Hinge-Motion in Proteins". En ASME 2000 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2000. http://dx.doi.org/10.1115/imece2000-2634.
Texto completoInformes sobre el tema "Proteins - Conformation Dynamics"
Hanke, Andreas. Studies of Single Biomolecules, DNA Conformational Dynamics, and Protein Binding. Fort Belvoir, VA: Defense Technical Information Center, julio de 2008. http://dx.doi.org/10.21236/ada483440.
Texto completoMarkelz, Andrea G. Terahertz Time Domain Spectroscopy of Conformational Dynamics of Sensor Proteins: Basic Research and Pathogen Sensor Development. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2004. http://dx.doi.org/10.21236/ada426482.
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