Modulation of allostery by protein intrinsic disorder - Nature.com
Modulation of allostery by protein intrinsic disorder - Nature.com
Modulation of allostery by protein intrinsic disorder Nature.com
Previous attempts at measuring dissociation constants (Kd) for E1A complexes with CBP by isothermal titration calorimetry (ITC) and nuclear magnetic resonance (NMR) failed because E1A is highly aggregation-prone. Even at concentrations as low as 10 μM ...
NMR insights into protein allostery
NMR insights into protein allostery
15 March 2012
Publication year: 2012
Source:Archives of Biochemistry and Biophysics, Volume 519, Issue 2</br>
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Allosterism is one of nature’s principal methods for regulating protein function. Allosterism utilizes ligand binding at one site to regulate the function of the protein by modulating the structure and dynamics of a distant binding site. In this review, we first survey solution NMR techniques and how they may be applied to the study of allostery. Subsequently, we describe several examples of application of NMR to protein...
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[NMR paper] Protein function and allostery: a dynamic relationship.
From Mendeley Biomolecular NMR group:
Protein function and allostery: a dynamic relationship.
Annals of the New York Academy of Sciences (2012). Pages: 1-6. Charalampos G Kalodimos et al.
Allostery is a fundamental process by which distant sites within a protein system sense each other. Allosteric regulation is such an efficient mechanism that it is used to control protein activity in most biological processes, including signal transduction, metabolism, catalysis, and gene regulation. Over recent years, our view and understanding of the fundamental principles underlying allostery...
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10-12-2012 09:58 AM
[NMR paper] Protein function and allostery: a dynamic relationship.
From Mendeley Biomolecular NMR group:
Protein function and allostery: a dynamic relationship.
Annals of the New York Academy of Sciences (2012). Pages: 1-6. Charalampos G Kalodimos et al.
Allostery is a fundamental process by which distant sites within a protein system sense each other. Allosteric regulation is such an efficient mechanism that it is used to control protein activity in most biological processes, including signal transduction, metabolism, catalysis, and gene regulation. Over recent years, our view and understanding of the fundamental principles underlying allostery...
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] Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues
Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.
Related Articles Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.
J Mol Biol. 1998 Dec 18;284(5):1597-609
Authors: Griffiths-Jones SR, Sharman GJ, Maynard AJ, Searle MS
Analysis of residues in coil regions of protein structures...
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11-17-2010 11:15 PM
Detect protein disorder to avoid wasting NMR time
Unless disordered proteins is what you are after, you may want to check if the protein you want to study with NMR is actually disordered and most likely not a very good NMR target.
The following servers for prediction of disordered regions in proteins are available. PONDR
DisEMBL
Globplot2
DISOPRED2
PDISORDER
PredictProtein
Modulation of allostery by protein intrinsic disorder - Nature.com
Linear Mode
