Related ArticlesInsights into the local residual entropy of proteins provided by NMR relaxation.
Protein Sci. 1996 Dec;5(12):2647-50
Authors: Li Z, Raychaudhuri S, Wand AJ
A simple model is used to illustrate the relationship between the dynamics measured by NMR relaxation methods and the local residual entropy of proteins. The expected local dynamic behavior of well-packed extended amino acid side chains are described by employing a one-dimensional vibrator that encapsulates both the spatial and temporal character of the motion. This model is then related to entropy and to the generalized order parameter of the popular "model-free" treatment often used in the analysis of NMR relaxation data. Simulations indicate that order parameters observed for the methyl symmetry axes in, for example, human ubiquitin correspond to significant local entropies. These observations have obvious significance for the issue of the physical basis of protein structure, dynamics, and stability.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 05:59 AM
[NMR paper] Relating side-chain mobility in proteins to rotameric transitions: insights from mole
Relating side-chain mobility in proteins to rotameric transitions: insights from molecular dynamics simulations and NMR.
Related Articles Relating side-chain mobility in proteins to rotameric transitions: insights from molecular dynamics simulations and NMR.
J Biomol NMR. 2005 Jun;32(2):151-62
Authors: Hu H, Hermans J, Lee AL
The dynamic aspect of proteins is fundamental to understanding protein stability and function. One of the goals of NMR studies of side-chain dynamics in proteins is to relate spin relaxation rates to discrete...
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11-25-2010 08:21 PM
[NMR paper] Probing residual interactions in unfolded protein states using NMR spin relaxation te
Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta.
Related Articles Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta.
J Am Chem Soc. 2003 Oct 1;125(39):11988-92
Authors: Choy WY, Kay LE
Residual interactions in delta131delta, a large disordered fragment of staphylococcal nuclease, have been probed at two different pHs using backbone (15)N and side-chain methyl (2)H NMR spin relaxation...
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11-24-2010 09:16 PM
[NMR paper] Thermodynamic insights into proteins from NMR spin relaxation studies.
Thermodynamic insights into proteins from NMR spin relaxation studies.
Related Articles Thermodynamic insights into proteins from NMR spin relaxation studies.
Curr Opin Struct Biol. 2001 Oct;11(5):555-9
Authors: Spyracopoulos L, Sykes BD
NMR spin relaxation measurements of picosecond to nanosecond timescale backbone and sidechain fluctuations of protein molecules, and subsequent entropic interpretation yield interesting, but sometimes counterintuitive, insights into proteins. The stabilities of proteins and protein interactions are achieved...
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11-19-2010 08:44 PM
[NMR paper] NMR relaxation studies of the role of conformational entropy in protein stability and
NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Related Articles NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Acc Chem Res. 2001 May;34(5):379-88
Authors: Stone MJ
Recent advances in the measurement and analysis of protein NMR relaxation data have made it possible to characterize the dynamical properties of many backbone and side chain groups. With certain caveats, changes in flexibility that occur upon ligand binding, mutation, or...
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11-19-2010 08:32 PM
[NMR paper] Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics.
Related Articles Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics.
Biochemistry. 2001 Mar 6;40(9):2743-53
Authors: Viles JH, Donne D, Kroon G, Prusiner SB, Cohen FE, Dyson HJ, Wright PE
A template-assisted conformational change of the cellular prion protein (PrP(C)) from a predominantly helical structure to an amyloid-type structure with a higher proportion of beta-sheet is thought to be the causative factor in prion...
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11-19-2010 08:32 PM
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov
Journal of Biomolecular NMR; 2007; 39(1) pp 1-16
Abstract:
A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...
Insights into the local residual entropy of proteins provided by NMR relaxation.
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