Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
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[NMR paper] Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Related Articles Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Protein Pept Lett. 2005 Apr;12(3):235-40
Authors: Spyracopoulos L
Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain (2)H and (13)C, and backbone (15)N nuclei using NMR spectroscopy. The rates reflect protein motions on timescales from picoseconds to milliseconds. Backbone and methyl side chain NMR...
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11-25-2010 08:21 PM
[NMR paper] Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on B
Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations.
Related Articles Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations.
J Biomol NMR. 2004 May;29(1):21-35
Authors: Bernadó P, Fernandes MX, Jacobs DM, Fiebig K, García de la Torre J, Pons M
Many important proteins contain multiple domains connected by flexible linkers. Inter-domain motion is suggested to play a key role in many processes involving molecular recognition....
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11-24-2010 09:51 PM
[NMR paper] New approaches to the dynamic interpretation and prediction of NMR relaxation data fr
New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins.
Related Articles New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins.
Curr Opin Struct Biol. 2003 Apr;13(2):175-83
Authors: Brüschweiler R
NMR relaxation experiments of isotopically labeled proteins provide a wealth of information on reorientational global and local dynamics on nanosecond and subnanosecond timescales for folded and nonfolded proteins in solution. Recent methodological advances in the...
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11-24-2010 09:01 PM
[NMR paper] Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic cal
Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR.
Related Articles Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR.
J Biomol NMR. 2002 Jun;23(2):139-50
Authors: Bernadó P, García de la Torre J, Pons M
HYDRONMR is an implementation of state of the art hydrodynamic modeling to calculate the spectral density functions for NH or C(alpha)-H vectors in a rigid protein structure starting from an atomic level representation. Thus...
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11-24-2010 08:49 PM
[NMR paper] Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Related Articles Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Biochemistry. 1995 Apr 18;34(15):5212-23
Authors: Zheng Z, Czaplicki J, Jardetzky O
Backbone dynamics of trp repressor, a 25 kDa DNA binding protein, have been studied using 15N relaxation data measured by proton-detected two-dimensional 1H-15N NMR spectroscopy. 15N spin-lattice relaxation time (T1), spin-spin relaxation time (T2), and heteronuclear NOEs were determined for all visible backbone...
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[NMR paper] Collective NMR relaxation model applied to protein dynamics.
Collective NMR relaxation model applied to protein dynamics.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/-PMGifs-Toolbar-topub.gif Related Articles Collective NMR relaxation model applied to protein dynamics.
Phys Rev Lett. 1994 Feb 7;72(6):940-943
Authors: Brüschweiler R, Case DA
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2H NMR Spin Relaxation for studying RNA dynamics
A Suite of 2H NMR Spin Relaxation Experiments for the Measurement of RNA Dynamics
Pramodh Vallurupalli and Lewis E. Kay, J. Am. Chem. Soc.; 2005; 127 (18) pp 6893 - 6901
ABSTRACT:
A suite of (2)H-based spin relaxation NMR experiments is presented for the measurement of molecular dynamics in a site-specific manner in uniformly (13)C, randomly fractionally deuterated ( approximately 50%) RNA molecules. The experiments quantify (2)H R(1) and R(2) relaxation rates that can subsequently be analyzed to obtain information about dynamics on a pico- to nanosecond time scale. Sensitivity...
The Dynamics of Dendrimers by NMR Relaxation: Interpretation Pitfalls
Linear Mode
