Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at unprecedented detail, revealing intriguing aspects of allosteric mechanisms and increasing the proportion of the conformational ensemble that can be observed by experiment. Here, we present an overview of NMR spectroscopic methods for characterizing equilibrium fluctuations in free and bound states of allosteric proteins that have been most influential in the field. By combining NMR experimental approaches with molecular simulations, atomistic-level descriptions of the mechanisms by which allosteric phenomena take place are now within reach.
PMID: 26964042 [PubMed - as supplied by publisher]
[NMR paper] Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Related Articles Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Chem Rev. 2016 Jan 6;
Authors: Lisi GP, Loria JP
Abstract
Allostery is a ubiquitous biological regulatory process in which distant binding sites within a protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions play essential roles in many enzymological mechanisms, often facilitating formation of enzyme-substrate complexes and/or product release. Thus,...
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01-07-2016 11:10 PM
[NMR paper] NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions.
NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions.
Adv Exp Med Biol. 2014;805:271-304
Authors: Ghitti M, Musco G, Spitaleri A
Abstract
The recurrent failures in drug discovery campaigns, the asymmetry between the...
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05-31-2014 01:47 AM
[NMR paper] Solution NMR and Computational Methods for Understanding Protein Allostery.
Solution NMR and Computational Methods for Understanding Protein Allostery.
Solution NMR and Computational Methods for Understanding Protein Allostery.
J Phys Chem B. 2013 Feb 26;
Authors: Manley GA, Rivalta I, Loria JP
Abstract
Allosterism is an essential biological regulatory mechanism. In enzymes, allosteric regulation results in an activation or inhibition of catalytic turnover. The mechanisms by which this is accomplished are unclear and vary significantly depending on the enzyme. It is commonly the case that a metabolite binds to...
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03-01-2013 09:57 PM
[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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01-21-2013 02:09 PM
[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...
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09-06-2012 01:42 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...
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08-24-2012 08:01 PM
[MWClarkson blog] Dynamic origins of PBX1 homeodomain allostery
Dynamic origins of PBX1 homeodomain allostery
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngIn the Monod-Wyman-Changeux model for cooperative binding, proteins exist in an equilibrium of low-affinity and high-affinity states in solution, absent any ligand. In this view, although it may appear that the binding of a ligand causes a conformational transition, it actually stabilizes one conformation from a pre-existing equilibrium. In the past several years, advanced NMR techniques have yielded increasing evidence that these structural equilibria exist for a number of...
NMR Methods to Study Dynamic Allostery.
Linear Mode
