Publication date: Available online 14 March 2017 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Liliya Vugmeyster, Dmitry Ostrovsky
In this review, we discuss the experimental static deuteron NMR techniques and computational approaches most useful for the investigation of side-chain dynamics in protein systems. Focus is placed on the interpretation of line shape and relaxation data within the framework of motional modeling. We consider both jump and diffusion models and apply them to uncover glassy behaviors, conformational exchange and dynamical transitions in proteins. Applications are chosen from globular and membrane proteins, amyloid fibrils, peptide adsorbed on surfaces and proteins specific to connective tissues. Graphical abstract
A Studyof Phenylalanine Side-Chain Dynamics in Surface-AdsorbedPeptides Using Solid-State Deuterium NMR and Rotamer Library Statistics
A Studyof Phenylalanine Side-Chain Dynamics in Surface-AdsorbedPeptides Using Solid-State Deuterium NMR and Rotamer Library Statistics
Kun Li, Prashant S. Emani, Jason Ash, Michael Groves and Gary P. Drobny
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504677d/aop/images/medium/ja-2014-04677d_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504677d
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08-06-2014 07:59 AM
[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
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
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
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01-13-2011 12:00 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...
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11-18-2010 09:15 PM
[NMR paper] Solid-state NMR studies of proteins: the view from static 2H NMR experiments.
Solid-state NMR studies of proteins: the view from static 2H NMR experiments.
Related Articles Solid-state NMR studies of proteins: the view from static 2H NMR experiments.
Biochem Cell Biol. 1998;76(2-3):411-22
Authors: Siminovitch DJ
The application of solid-state 2H NMR spectroscopy to the study of protein and peptide structure and dynamics is reviewed. The advantages of solid-state NMR for the study of proteins are considered, and the particular advantages of solid-state 2H NMR are summarized. Examples of work on the integral membrane...
Static Solid-state 2H NMR Methods in Studies of Protein Side-chain Dynamics
Linear Mode
