Related ArticlesDynamic activation of protein function: a view emerging from NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):926-31
Authors: Wand AJ
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion to report on the residual conformational entropy of proteins and how this entropy can enter into both the thermodynamic and kinetic aspects of protein function.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
J Magn Reson. 2011 Mar 30;
Authors: Kay LE
With the development of appropriate labeling schemes and the associated experiments that exploit them it has become possible to record high quality solution NMR spectra of supra-molecular complexes with molecular masses extending to 1MDa. One such approach involves selective (13)CH(3) methyl labeling in highly deuterated proteins...
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Solution NMR Spectroscopy of Supra-Molecular Systems, Why Bother? A Methyl TROSY View
Solution NMR Spectroscopy of Supra-Molecular Systems, Why Bother? A Methyl TROSY View
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 8 March 2011</br>
Lewis E., Kay</br>
With the development of appropriate labeling schemes and the associated experiments that exploit them it has become possible to record high quality solution NMR spectra of supra-molecular complexes with molecular masses extending to 1MDa. One such approach involves selective 13CH3 methyl labeling in highly deuterated proteins using experiments that make...
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[NMR paper] An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
Related Articles An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
Magn Reson Med Sci. 2002;1(1):27-31
Authors: Kuwata K
A new concept of protein dynamics has emerged quite recently, and a crucial link between protein dynamics and function has been largely established using recent NMR techniques in the solution state. Protein structure is governed by the thermodynamic principle and may not necessarily be unique in the...
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11-24-2010 08:49 PM
[NMR images] View this protein\x26#39;s PDB entry
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[NMR paper] Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Related Articles Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Toxicol Lett. 1995 Dec;82-83:577-89
Authors: Hsu VL, Jia X, Kearns DR
The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to...
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[NMR paper] Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated co
Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc-MS.gif Related Articles Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.
J Biol Chem. 1993 Jun 25;268(18):13081-8
Authors: Drake SK, Bourret RB, Luck LA, Simon MI, Falke JJ
CheY, the 14-kDa response regulator protein of...
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08-21-2010 11:53 PM
[NMR paper] 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by
19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-.
Related Articles 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-.
J Biol Chem. 1991 Feb 25;266(6):3396-401
Authors: Higashijima T, Graziano MP, Suga H, Kainosho M, Gilman AG
19F and 31P NMR spectroscopy was used to study the mechanism of activation of the alpha subunits of guanine nucleotide-binding regulatory proteins (G proteins) by Al3+, Mg2+, and F-. 19F NMR spectra of solutions containing Al3+,...
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Structure and function of G protein-coupled receptors using NMR spectroscopy
Structure and function of G protein-coupled receptors using NMR spectroscopy
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 12 May 2010</br>
Joseph A., Goncalves , Shivani, Ahuja , Sina, Erfani , Markus, Eilers , Steven O., Smith</br>
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Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Linear Mode
