[NMR paper] Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.
Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.
J Am Chem Soc. 2015 Dec 11;
Authors: Rosenzweig R, Kay LE
Abstract
Solution-based NMR spectroscopy has been an important tool for studying the structure and dynamics of relatively small proteins and protein complexes with aggregate molecular masses under approximately 50 kDa. The development of new experiments and labeling schemes, coupled with continued improvements in hardware, has significantly reduced this size limitation, enabling atomic resolution studies of molecular machines in the 1 MDa range. In this perspective some of the important advances are highlighted in the context of studies of molecular chaperones involved in protein disaggregation. New insights into the structural biology of disaggregation obtained from NMR studies are described, focusing on the unique capabilities of the methodology for obtaining atomic resolution descriptions of dynamic systems.
PMID: 26651836 [PubMed - as supplied by publisher]
[NMR paper] (13)CHD 2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.
(13)CHD 2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.
Related Articles (13)CHD 2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.
J Biomol NMR. 2015 Aug 14;
Authors: Rennella E, Huang R, Velyvis A, Kay LE
Abstract
An NMR experiment for quantifying slow (millisecond) time-scale exchange processes involving the interconversion between visible ground state and invisible, conformationally excited...
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08-15-2015 04:01 PM
13 CHD 2 â??CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins
13 CHD 2 â??CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins
Abstract
An NMR experiment for quantifying slow (millisecond) time-scale exchange processes involving the interconversion between visible ground state and invisible, conformationally excited state conformers is presented. The approach exploits chemical exchange saturation transfer (CEST) and makes use of 13CHD2 methyl group probes that can be readily incorporated into otherwise highly deuterated proteins. The methodology is...
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08-14-2015 10:12 PM
[NMR paper] Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR.
Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR.
Related Articles Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR.
Annu Rev Biochem. 2014 Jun 2;83:291-315
Authors: Rosenzweig R, Kay LE
Abstract
Large macromolecular assemblies, so-called molecular machines, are critical to ensuring proper cellular function. Understanding how proper function is achieved at the atomic level is crucial to advancing multiple avenues of biomedical research. Biophysical studies often include X-ray diffraction and...
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06-07-2014 07:12 PM
Big Data Tackles Tiny Molecular Machines - Science 2.0
<img alt="" height="1" width="1" />
Big Data Tackles Tiny Molecular Machines
Science 2.0
"Structural techniques like X-ray crystallography and nuclear magnetic resonance have worked quite well to help us understand how smaller proteins function," Onuchic said. X-rays only take snapshots of constantly moving proteins, he said, "but ...
Big Data Tackles Tiny Molecular Machines - Science 2.0
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03-16-2014 02:03 AM
New technique to analyze conformations of complex molecular machines - Phys.Org
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcRo1TkQ4r1fMpUxa3wD5SK2d2V8T_oG2l78aZVQEcL_XDMCV_pyy0Biarzf0xAik6wok_0CyH8
Phys.Org
<img alt="" height="1" width="1" />
New technique to analyze conformations of complex molecular machines
Phys.Org
"Structural techniques like X-ray crystallography and nuclear magnetic resonance have worked quite well to help us understand how smaller proteins function," Onuchic said. X-rays only take snapshots of constantly moving proteins, he said, "but ...
and more »
New technique to analyze conformations of complex molecular machines...
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03-14-2014 07:34 PM
[NMR paper] Structural Investigations of Molecular Machines by Solid-State NMR.
Structural Investigations of Molecular Machines by Solid-State NMR.
Related Articles Structural Investigations of Molecular Machines by Solid-State NMR.
Acc Chem Res. 2013 Mar 15;
Authors: Loquet A, Habenstein B, Lange A
Abstract
Essential biological processes such as cell motion, signaling,protein synthesis, and pathogen-host interactions rely on multifunctional molecular machines containing supramolecular assemblies, that is, noncovalently assembled protein subunits. Scientists would like to acquire a detailed atomic view of the complete...
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03-19-2013 01:22 PM
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Andrew J. Baldwin, Patrick Walsh, D. Flemming Hansen, Gillian R. Hilton, Justin L. P. Benesch, Simon Sharpe and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307874r/aop/images/medium/ja-2012-07874r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307874r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qcs9RnHBiBY
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Solution NMR Evidence for Symmetry in Functionally or Crystallographically Asymmetric Homodimers
Solution NMR Evidence for Symmetry in Functionally or Crystallographically Asymmetric Homodimers
Raquel Godoy-Ruiz, Anna Krejcirikova, D. Travis Gallagher and Vitali Tugarinov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206967d/aop/images/medium/ja-2011-06967d_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206967d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Y_QrFWfv--4