Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR [Biophysics and Computational Biology]
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
Kato, H., van Ingen, H., Zhou, B.-R., Feng, H., Bustin, M., Kay, L. E., Bai, Y....
Date: 2011-07-26
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility group nucleosomal (HMGN) protein family that regulates various chromatin functions, including transcription. Here, we report the architecture of the HMGN2-nucleosome...
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07-26-2011 11:22 PM
Current Applications of 19F NMR to Studies of Protein Structure and Dynamics
Current Applications of 19F NMR to Studies of Protein Structure and Dynamics
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 13 July 2011</br>
Julianne L., Kitevski-LeBlanc , R., Scott Prosser</br>
*Highlights:*? 19F molecular tags and labelling protocols for 19F NMR studies of proteins are reviewed and contrasted. ? 19F NMR biosynthetic labelling strategies are presented. ? Experimental challenges (loss of function through labelling, line broadening, assignment ambiguities) are discussed. ?...
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07-14-2011 08:55 PM
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Proc Natl Acad Sci U S A. 2011 Jul 5;
Authors: Kato H, van Ingen H, Zhou BR, Feng H, Bustin M, Kay LE, Bai Y
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility...
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07-07-2011 05:12 PM
1H NMR Chemical Shift Calculations as a Probe of Supramolecular Host–Guest Geometry
1H NMR Chemical Shift Calculations as a Probe of Supramolecular Host–Guest Geometry
Jeffrey S. Mugridge, Robert G. Bergman and Kenneth N. Raymond
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202254x/aop/images/medium/ja-2011-02254x_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202254x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/wR-1b5WtJhc
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06-30-2011 05:01 AM
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
J Am Chem Soc. 2011 May 11;
Authors: Religa TL, Ruschak AM, Rosenzweig R, Kay LE
Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
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05-12-2011 03:40 PM
[NMR paper] Structural consequences of site-directed mutagenesis in flexible protein domains: NMR
Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.
Related Articles Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.
Eur J Biochem. 2001 Apr;268(8):2253-60
Authors: Golovanov AP, Hawkins D, Barsukov I, Badii R, Bokoch GM, Lian LY, Roberts GC
The guanine dissociation inhibitor RhoGDI consists of a folded C-terminal domain and a highly flexible N-terminal region, both of...
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11-19-2010 08:32 PM
Optimal methyl labeling for studies of supra-molecular systems
Abstract Selective methyl labeling combined with HMQC spectroscopy that exploits a TROSY effect in 13CH3 spin systems has significantly extended the utility of solution NMR spectroscopy in studies of high molecular weight particles. Herein we compare the utility of 13CH3- versus 13CHD2-labeling of Ile, Leu, Val probes in supra-molecular systems through quantification of relative signal-to-noise ratios in optimized spectra of highly deuterated, 13CH3- and 13CHD2-labeled samples of the half proteasome (α7α7, 360 kDa). It is shown that the sensitivity of spectra recorded on Ile, Leu, Val...
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08-14-2010 04:19 AM
A new spin probe of protein dynamics
A new spin probe of protein dynamics: nitrogen relaxation in (15)n-(2)h amide groups.
Xu J, Millet O, Kay LE, Skrynnikov NR.
Contribution from the Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, and Departments of Medical Genetics, Biochemistry, and Chemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
J Am Chem Soc. 2005 Mar 9;127(9):3220-9.
(15)N spin relaxation data have provided a wealth of information on protein dynamics in solution. Standard R(1), R(1)(rho), and NOE experiments aimed at (15)N amide moieties are complemented in this...
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
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