[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...
nmrlearner
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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...
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12-02-2010 08:41 AM
[NMR paper] Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GM
Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
Biochemistry. 1997 Apr 22;36(16):5045-52
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational changes between the GMPPNP form of human N-ras P21...
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08-22-2010 03:31 PM
[NMR paper] Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GM
Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
Biochemistry. 1997 Apr 22;36(16):5045-52
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational changes between the GMPPNP form of human N-ras P21...
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08-22-2010 03:03 PM
[NMR paper] Dynamic properties of proteins from NMR spectroscopy.
Dynamic properties of proteins from NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Dynamic properties of proteins from NMR spectroscopy.
Curr Opin Biotechnol. 1993 Aug;4(4):385-91
Authors: Palmer AG
Two-dimensional proton-detected heteronuclear nuclear magnetic resonance spectroscopy has been used to measure 13C and 15N spin-relaxation rate constants for several proteins. Generalized order parameters and effective internal correlation times have been...
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08-22-2010 03:01 AM
Structural biology: Molecular machinery in action
News and Views
Nature 445, 609 (8 February 2007) | <abbr title="Digital Object Identifier">doi</abbr>:10.1038/nature05566; Published online 21 January 2007
Structural biology: Molecular machinery in action
Ad Bax and Dennis A. Torchia
Abstract