[NMR paper] Mapping the energy landscape of protein-ligand binding via linear free energy relationships determined by protein NMR relaxation dispersion
Biochemical signaling is mediated by complexes between macromolecular receptors and their ligands, with the duration of the signal being directly related to the lifetime of the ligand-receptor complex. In the field of drug design, the recognition that drug efficacy in vivo depends on the lifetime of the drug-protein complex has spawned the concept of designing drugs with particular binding kinetics. To advance this field it is critical to investigate how the molecular details of designed ligands...
Characterization of Protein Kinase a Free Energy Landscape by NMR-Restrained Metadynamics
Characterization of Protein Kinase a Free Energy Landscape by NMR-Restrained Metadynamics
Publication date: 3 February 2017
Source:Biophysical Journal, Volume 112, Issue 3, Supplement 1</br>
Author(s): Yingjie Wang, Carlo Camilloni, Jonggul Kim, Michele Vendruscolo, Jiali Gao, Gianluigi Veglia</br>
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02-03-2017 09:55 PM
[NMR paper] Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Phys Chem Chem Phys. 2017 Jan 09;:
Authors: Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M
Abstract
RNA molecules in solution tend to undergo structural fluctuations of...
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01-12-2017 03:48 AM
[NMR paper] The Complexity of Protein Energy Landscapes Studied by Solution NMR Relaxation Dispersion Experiments.
The Complexity of Protein Energy Landscapes Studied by Solution NMR Relaxation Dispersion Experiments.
Related Articles The 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...
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02-14-2015 03:52 PM
[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, Muņoz 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
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Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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01-18-2011 10:22 PM
[NMR paper] The pressure-temperature free energy-landscape of staphylococcal nuclease monitored b
The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
Related Articles The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
J Mol Biol. 2000 Apr 28;298(2):293-302
Authors: Lassalle MW, Yamada H, Akasaka K
The thermodynamic stability of staphylococcal nuclease was studied against the variation of both temperature and pressure by utilizing (1)H NMR spectroscopy at 750 MHz in 20 mM Mes buffer containing 99.9 % (2)H(2)O, pH 5.3. Equilibrium fractions of folded...