[NMR paper] A Study of Phenylalanine Side Chain Dynamics in Surface-Adsorbed Peptides Using Solid State Deuterium NMR and Rotamer Library Statistics.
A Study of Phenylalanine Side Chain Dynamics in Surface-Adsorbed Peptides Using Solid State Deuterium NMR and Rotamer Library Statistics.
A Study of Phenylalanine Side Chain Dynamics in Surface-Adsorbed Peptides Using Solid State Deuterium NMR and Rotamer Library Statistics.
J Am Chem Soc. 2014 Jul 23;
Authors: Li K, Emani PS, Ash J, Groves M, Drobny GP
Abstract
Extracellular matrix proteins adsorbed onto mineral surfaces exist in a unique environment where the structure and dynamics of the protein can be altered...
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07-24-2014 11:56 AM
Proton Clouds to Measure Long-Range Contacts between Nonexchangeable Side Chain Protons in Solid-State NMR
Proton Clouds to Measure Long-Range Contacts between Nonexchangeable Side Chain Protons in Solid-State NMR
Tessa Sinnige, Mark Danie?ls, Marc Baldus and Markus Weingarth
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja412870m/aop/images/medium/ja-2013-12870m_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja412870m
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/0gtd6wPcuVY
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01-31-2014 06:44 PM
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 16;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21928443
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09-20-2011 03:10 PM
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 14;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21915969
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09-15-2011 08:31 PM
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.
J Biomol NMR. 2011 Aug 7;
Authors: Linser R
Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange...
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08-09-2011 12:11 PM
[NMR paper] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r
Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
Related Articles Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
J Am Chem Soc. 2005 Jun 8;127(22):8214-25
Authors: Tugarinov V, Ollerenshaw JE, Kay LE
New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...
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11-25-2010 08:21 PM
[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Related Articles Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
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11-19-2010 08:32 PM
[NMR paper] Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumi
Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study.
Related Articles Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study.
Biochemistry. 2000 Jan 18;39(2):372-80
Authors: Bai P, Luo L, Peng Z
The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a prototype of partially folded proteins. Despite the importance of molten globules in understanding the mechanisms of protein folding and its relevance to some biological...