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 reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes...
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01-21-2016 01:08 PM
[NMR paper] NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Related Articles NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Protein Sci. 2016 Jan 8;
Authors: Mohanty B, Geralt M, Wüthrich K, Serrano P
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence...
nmrlearner
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01-11-2016 03:57 PM
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes...
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01-09-2016 04:06 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...
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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...
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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...
nmrlearner
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08-24-2012 08:01 PM
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...
Adding Substituent Nonadditivity in Protein Allostery by NMR.
Linear Mode
