This review surveys recent investigations of conformational fluctuations of proteins in solution using NMR techniques. Advances in experimental methods have provided more accurate means of characterizing fast and slow internal motions as well as overall diffusion. The information obtained from NMR dynamics experiments provides insights into specific structural changes or configurational energetics associated with function. A variety of applications illustrate that studies of protein dynamics provide insights into protein-protein interactions, target recognition, ligand binding, and enzyme function.
NMR studies of protein structure and dynamics
NMR studies of protein structure and dynamics
Publication year: 2011
Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 477-491</br>
Lewis E.*Kay</br>
Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100*kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is provided in a study of...
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12-11-2011 07:57 AM
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
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03-23-2011 05:41 PM
[NMR structure and dynamics of the chimeric protein SH3-F2].
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Mol Biol (Mosk). 2010 Nov-Dec;44(6):1064-74
Authors:
For the further elucidation of structural and dynamic principles of protein self-organization and protein-ligand interactions the design of new chimeric protein SH3-F2 was made and genetically engineered construct was created. The SH3-F2 amino acid sequence consists of polyproline ligand mgAPPLPPYSA, GG linker and the sequence of spectrin SH3 domain circular permutant S19-P20s. Structural and dynamics properties of the protein were studied by high-resolution NMR. According to NMR data the...
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02-05-2011 05:28 PM
Protein dynamics and allostery: an NMR view.
Protein dynamics and allostery: an NMR view.
Related Articles Protein dynamics and allostery: an NMR view.
Curr Opin Struct Biol. 2010 Nov 23;
Authors: Tzeng SR, Kalodimos CG
Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link...
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11-27-2010 02:45 PM
[NMR paper] NMR studies of protein structure and dynamics.
NMR studies of protein structure and dynamics.
Related Articles NMR studies of protein structure and dynamics.
J Magn Reson. 2005 Apr;173(2):193-207
Authors: Kay LE
Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100 kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is...
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11-25-2010 08:21 PM
[NMR paper] Protein dynamics from NMR.
Protein dynamics from NMR.
Related Articles Protein dynamics from NMR.
Nat Struct Biol. 1998 Jul;5 Suppl:513-7
Authors: Kay LE
In the past several years a significant number of new multidimensional NMR methods have been developed to study molecular dynamics spanning a wide range of time scales. Applications involving a large number of biological systems have emerged and correlations with function established. Unique insights are obtained that are not available from structure alone, indicating the importance of dynamics studies for...
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11-17-2010 11:15 PM
[NMR paper] Protein dynamics from NMR.
Protein dynamics from NMR.
Related Articles Protein dynamics from NMR.
Biochem Cell Biol. 1998;76(2-3):145-52
Authors: Kay LE
The past several years have seen the development of a significant number of new multidimensional NMR methods for the study of molecular dynamics spanning a wide range of time scales. Applications involving a large number of different biological systems have emerged and correlations with function have been established. Unique insights are obtained that are not available from structure alone, indicating the importance of...
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11-17-2010 11:06 PM
A new spin probe of protein dynamics
A new spin probe of protein dynamics: nitrogen relaxation in (15)n-(2)h amide groups.
Xu J, Millet O, Kay LE, Skrynnikov NR.
Contribution from the Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, and Departments of Medical Genetics, Biochemistry, and Chemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
J Am Chem Soc. 2005 Mar 9;127(9):3220-9.
(15)N spin relaxation data have provided a wealth of information on protein dynamics in solution. Standard R(1), R(1)(rho), and NOE experiments aimed at (15)N amide moieties are complemented in this...
Protein dynamics from NMR.
Linear Mode
