Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Prion. 2011 Jul 1;5(3)
Authors: Santo KP, Berjanskii M, Wishart DS, Stepanova M
Abstract
Collective motions on ns-?s time scales are known to have a major impact on protein folding, stability, binding and enzymatic efficiency. It is also believed that these motions may have an...
nmrlearner
Journal club
0
08-27-2011 04:53 PM
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
nmrlearner
Journal club
0
03-23-2011 05:41 PM
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...
nmrlearner
Journal club
0
01-13-2011 12:00 PM
A Practical Guide to Protein Dynamics From 15N Spin Relaxation in Solution
A Practical Guide to Protein Dynamics From 15N Spin Relaxation in Solution
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 7 January 2011</br>
S. Bastien, Morin</br>
More...
nmrlearner
Journal club
0
01-08-2011 12:25 PM
[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...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-
Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
Related Articles Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
J Biomol Struct Dyn. 1999 Aug;17(1):157-74
Authors: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS
This paper presents a procedure for detection of intermediate nanosecond internal dynamics in globular proteins. The procedure uses 1H-15N relaxation measurements at several spectrometer frequencies...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[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
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the unc
15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Biochemistry. 1993 Sep 7;32(35):9000-10
Authors: Cheng JW, Lepre CA, Chambers SP, Fulghum JR, Thomson JA, Moore JM
Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy....
Collective NMR relaxation model applied to protein dynamics.
Linear Mode
