Related ArticlesRelaxation dispersion NMR spectroscopy for the study of protein allostery.
Biophys Rev. 2015 Jun;7(2):191-200
Authors: Farber PJ, Mittermaier A
Abstract
Allosteric transmission of information between distant sites in biological macromolecules often involves collective transitions between active and inactive conformations. Nuclear magnetic resonance (NMR) spectroscopy can yield detailed information on these dynamics. In particular, relaxation dispersion techniques provide structural, dynamic, and mechanistic information on conformational transitions occurring on the millisecond to microsecond timescales. In this review, we provide an overview of the theory and analysis of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiments and briefly describe their application to the study of allosteric dynamics in the homeodomain from the PBX transcription factor (PBX-HD). CPMG NMR data show that local folding (helix/coil) transitions in one part of PBX-HD help to communicate information between two distant binding sites. Furthermore, the combination of CPMG and other spin relaxation data show that this region can also undergo local misfolding, reminiscent of conformational ensemble models of allostery.
[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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[NMR paper] Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy.
Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy.
Related Articles Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy.
J Biomol NMR. 2015 Oct 17;
Authors: Konuma T, Harada E, Sugase K
Abstract
Protein dynamics plays important roles in many biological events, such as ligand binding and enzyme reactions. NMR is mostly used for investigating such protein dynamics in a site-specific...
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10-20-2015 09:44 PM
Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy
Extracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy
Abstract
Protein dynamics plays important roles in many biological events, such as ligand binding and enzyme reactions. NMR is mostly used for investigating such protein dynamics in a site-specific manner. Recently, NMR has been actively applied to large proteins and intrinsically disordered proteins, which are attractive research targets. However, signal overlap, which is often observed for such proteins, hampers accurate...
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10-18-2015 09:10 AM
[NMR paper] High resolution NMR study of T? magnetic relaxation dispersion. IV. Proton relaxation in amino acids and Met-enkephalin pentapeptide.
High resolution NMR study of T? magnetic relaxation dispersion. IV. Proton relaxation in amino acids and Met-enkephalin pentapeptide.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--link.aip.org-jhtml-linkto.gif Related Articles High resolution NMR study of T? magnetic relaxation dispersion. IV. Proton relaxation in amino acids and Met-enkephalin pentapeptide.
J Chem Phys. 2014 Oct 21;141(15):155101
Authors: Pravdivtsev AN, Yurkovskaya AV, Vieth HM, Ivanov KL
Abstract
Nuclear Magnetic Relaxation Dispersion...
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10-06-2015 10:39 PM
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Measuring (1)H (N) temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
J Biomol NMR. 2011 Mar 18;
Authors: Bouvignies G, Vallurupalli P, Cordes MH, Hansen DF, Kay LE
A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated 'invisible' protein states that exchange...
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03-23-2011 05:41 PM
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy
Abstract A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated â??invisibleâ?? protein states that exchange with a â??visibleâ?? ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold...
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03-22-2011 07:32 PM
[NMR paper] An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mu
An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
Related Articles An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
J Am Chem Soc. 2005 Apr 13;127(14):5066-72
Authors: Choy WY, Zhou Z, Bai Y, Kay LE
15N relaxation dispersion NMR spectroscopy has been used to study exchange dynamics in a pair of mutants of Rd-apocyt b562, a redesigned four-helix-bundle protein. An analysis of the relaxation data over a range of...
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11-25-2010 08:21 PM
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
D. Flemming Hansen, Pramodh Vallurupalli and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 41(3); pp 113 - 120
Abstract:
Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part correspond to low energy (ground state) conformations. However, it is becoming increasingly well recognized that higher energy structures often play important roles in function as well. Because these conformers...
Relaxation dispersion NMR spectroscopy for the study of protein allostery.
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