Mucosa-associated lymphoid tissue lymphoma-translocation protein 1 (MALT1) is an attractive target for the development of modulatory compounds in the treatment of lymphoma and other cancers. While the three-dimensional structure of MALT1 has been previously determined through X-ray analysis, its dynamic behaviour in solution has remained unexplored. We present here dynamic analyses of the apo MALT1 form along with the E549A mutation. This investigation used NMR ^(15)N relaxation and NOE...
[NMR paper] Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold
Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold
RNase Y is a crucial component of genetic translation, acting as the key enzyme initiating mRNA decay in many Gram-positive bacteria. The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact with various protein partners within a degradosome complex. Bioinformatics and biophysical analysis have previously shown that Nter-BsRNaseY, which is in equilibrium between a monomeric and a dimeric form, displays an elongated fold with a high content of ?-helices. Using...
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12-23-2022 07:50 PM
[NMR paper] NMR Methods to Study Dynamic Allostery.
NMR Methods to Study Dynamic Allostery.
NMR Methods to Study Dynamic Allostery.
PLoS Comput Biol. 2016 Mar;12(3):e1004620
Authors: Grutsch S, Brüschweiler S, Tollinger M
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...
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03-11-2016 12:00 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...
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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...
nmrlearner
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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...
Insights into mechanisms of MALT1 allostery from NMR and AlphaFold dynamic analyses
Linear Mode
