[NMR paper] A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.
A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.
Related Articles A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA.
J Am Chem Soc. 2014 Feb 12;136(6):2204-7
Authors: Kannan A, Camilloni C, Sahakyan AB, Cavalli A, Vendruscolo M
Abstract
Recent improvements in the accuracy of structure-based methods for the prediction of...
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A ConformationalEnsemble Derived Using NMR MethylChemical Shifts Reveals a Mechanical Clamping Transition That Gatesthe Binding of the HU Protein to DNA
A ConformationalEnsemble Derived Using NMR MethylChemical Shifts Reveals a Mechanical Clamping Transition That Gatesthe Binding of the HU Protein to DNA
Arvind Kannan, Carlo Camilloni, Aleksandr B. Sahakyan, Andrea Cavalli and Michele Vendruscolo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4105396/aop/images/medium/ja-2013-105396_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4105396
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/I9LCRqDsIVA
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02-05-2014 04:40 AM
[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
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11-12-2012 01:53 AM
[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
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10-12-2012 09:58 AM
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Biophys J. 2011 Aug 3;101(3):L23-L25
Authors: Wang S, Shi L, Kawamura I, Brown LS, Ladizhansky V
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific...
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08-03-2011 12:00 PM
[NMR paper] Measuring pK(a) values in protein folding transition state ensembles by NMR spectrosc
Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
Related Articles Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
J Am Chem Soc. 2005 Jun 29;127(25):8904-5
Authors: Tollinger M, Kay LE, Forman-Kay JD
Protein folding kinetic data have been obtained for the marginally stable N-terminal SH3 domain of the Drosophila protein drk as a function of pH in order to investigate the electrostatic properties of Asp8 in the folding transition state ensemble. The slow exchange...
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11-25-2010 08:21 PM
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by t
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
Related Articles NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
FEBS Lett. 2010 Oct 8;
Authors: Lee EH, Seo YJ, Ahn HC, Kang YM, Kim HE, Lee YM, Choi BS, Lee JH
The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus,...
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10-13-2010 02:18 PM
[NMR paper] Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Annu Rev Biophys Biomol Struct. 1992;21:243-65
Authors: Englander SW, Mayne L
HX-labeling experiments in the pH-pulse mode show that protein folding can be remarkably fast. A near-native form can be reached within milliseconds. Experimental analysis of...
HighPressure ZZ-Exchange NMR Reveals Key Featuresof Protein Folding Transition States
Linear Mode
