Allostery is a fundamental mechanism of cellular homeostasis by intra-protein communication between distinct functional sites. It is an internal process of proteins to steer interactions not only with each other but also with other biomolecules such as ligands, lipids, and nucleic acids. In addition, allosteric regulation is particularly important in enzymatic activities. A major challenge in structural and molecular biology today is unraveling allosteric sites in proteins, to elucidate the...
Protein allostery and NMR - News-Medical.net
Protein allostery and NMR - News-Medical.net
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Protein allostery and NMR
News-Medical.net
Allostery â?? the phenomenon by which an event in one part of a molecule causes an effect in another â?? is a key feature of protein regulation in all living cells. Rather than directly affecting a protein's active site, allostery can modulate the active ...
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08-03-2016 05:31 PM
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...
nmrlearner
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02-03-2013 10:13 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...
nmrlearner
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10-12-2012 09:58 AM
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...
nmrlearner
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11-27-2010 02:45 PM
The war of tools: how can NMR spectroscopists detect errors in their structures?
The war of tools: how can NMR spectroscopists detect errors in their structures?
Edoardo Saccenti and Antonio Rosato
Journal of Biomolecular NMR; 2008; 40(4) pp 251 - 261
Abstract:
Protein structure determination by NMR methods has started in the mid-eighties and has been growing steadily since then. Ca. 14% of the protein structures deposited in the PDB have been solved by NMR. The evaluation of the quality of NMR structures however is still lacking a well-established practice. In this work, we examined various tools for the assessment of structural quality to ascertain the extent to...
linawaed
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08-04-2008 04:09 AM
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
NMR tools to detect protein allostery
Linear Mode
