Related ArticlesThe Complexity of Protein Energy Landscapes Studied by Solution NMR Relaxation Dispersion Experiments.
J Phys Chem B. 2015 Feb 13;
Authors: Khirich G, Loria JP
Abstract
The millisecond timescale motions in ribonuclease A (RNase A) were studied by solution NMR CPMG and off-resonance R1? relaxation dispersion experiments over a wide pH and temperature range. These experiments identify three separate protein regions termed Cluster 1, Cluster 2, and R33 whose motions are governed by distinct thermodynamic parameters. Moreover each of these regions has motions with different pH dependencies. Cluster 1 shows an increase in activation enthalpy and activation entropy as the pH is lowered, whereas Cluster two exhibits the opposite behavior. In contrast the activation enthalpy and entropy of R33 show no pH dependence. Compounding the differences, ?? values for Cluster 2 are characteristic of two-site conformational exchange yet similar analysis for Cluster 1 indicates that this region of the enzyme exhibits conformational fluctuations between a major conformer and a pH-dependent average of protonated and de-protonated minor conformers.
PMID: 25680027 [PubMed - as supplied by publisher]
[NMR paper] Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.
Related Articles Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.
J Am Chem Soc. 2014 May 8;
Authors: Sanchez-Medina C, Sekhar A, Vallurupalli P, Cerminara M, Muńoz V, Kay LE
Abstract
The topographic features of the free energy landscapes that govern the thermodynamics and kinetics of conformational transitions in proteins, which in turn are integral for function, are not well understood....
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05-09-2014 07:01 PM
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
Celia Sanchez-Medina, Ashok Sekhar, Pramodh Vallurupalli, Michele Cerminara, Victor Mun?oz and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja502705y/aop/images/medium/ja-2014-02705y_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja502705y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/uht26log5zQ
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[NMR paper] Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Chemphyschem. 2013 May 23;
Authors: Guerry P, Mollica L, Blackledge M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides detailed understanding of the nature and extent of protein dynamics on physiologically important timescales. We present recent advances in the combination of NMR with state-of-the-art molecular simulation that are providing unique new...
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05-25-2013 12:05 PM
[NMR paper] Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
Related Articles Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
Proc Natl Acad Sci U S A. 2013 Apr 9;
Authors: Granata D, Camilloni C, Vendruscolo M, Laio A
Abstract
The use of free-energy landscapes rationalizes a wide range of aspects of protein behavior by providing a clear illustration of the different states accessible to these molecules, as well as of their populations and pathways of interconversion. The...
Can Enzyme Engineering Benefit from the Modulation of Protein Motions? Lessons Learned from NMR Relaxation Dispersion Experiments.
Can Enzyme Engineering Benefit from the Modulation of Protein Motions? Lessons Learned from NMR Relaxation Dispersion Experiments.
Can Enzyme Engineering Benefit from the Modulation of Protein Motions? Lessons Learned from NMR Relaxation Dispersion Experiments.
Protein Pept Lett. 2011 Jan 11;
Authors:
Despite impressive progress in protein engineering and design, our ability to create new and efficient enzyme activities remains a laborious and time-consuming endeavor. In the past few years, intricate combinations of rational mutagenesis, directed...
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01-13-2011 12:00 PM
Suite of Six NMR Relaxation Dispersion Experiments to Study Multiple-Site Exchange in Proteins
http://pubs.acs.org/isubscribe/journals/jacsat/127/i44/figures/ja054550en00001.gif
Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments: An Application to the Folding of a Fyn SH3 Domain Mutant
Dmitry M. Korzhnev, Philipp Neudecker, Anthony Mittermaier, Vladislav Yu. Orekhov, and Lewis E. Kay*
Contribution from the Departments of Medical Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada, and Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden
J. Am. Chem....
The Complexity of Protein Energy Landscapes Studied by Solution NMR Relaxation Dispersion Experiments.
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