Publication date: Available online 19 December 2015 Source:Journal of Molecular Biology
Author(s): Lewis E. Kay
In the past several decades solution NMR spectroscopy has emerged as a powerful technique for the study of the structure and dynamics of proteins, providing detailed insights into biomolecular function. Herein I provide a summary of two important areas of application, focusing on NMR studies of (i) supra-molecular systems with aggregate molecular masses in the hundreds of kDa and of (ii) sparsely populated and transiently formed protein states that are thermally accessible from populated ground state conformations. The critical role of molecular dynamics in function is emphasized, highlighting the utility of the NMR technique in providing such often elusive information. Graphical abstract
[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.
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...
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Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins
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Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins
Valentine, K.G., et al., Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins. J Am Chem Soc, 2014. 136(7): p. 2800-7.
http://pubs.acs.org/doi/abs/10.1021/ja4107176
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03-27-2014 03:46 AM
ReverseMicelles As a Platform for Dynamic NuclearPolarization in Solution NMR of Proteins
ReverseMicelles As a Platform for Dynamic NuclearPolarization in Solution NMR of Proteins
Kathleen G. Valentine, Guinevere Mathies, Sabrina Be?dard, Nathaniel V. Nucci, Igor Dodevski, Matthew A. Stetz, Thach V. Can, Robert G. Griffin and A. Joshua Wand
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4107176/aop/images/medium/ja-2013-107176_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4107176
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02-05-2014 06:08 PM
[NMR paper] Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
Related Articles Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
J Am Chem Soc. 2014 Jan 24;
Authors: Valentine KG, Mathies G, Bédard S, Nucci NV, Dodevski I, Stetz MA, Can TV, Griffin RG, Wand AJ
Abstract
Despite tremendous advances in recent years, solution NMR remains fundamentally restricted due to its inherent insensitivity. Dynamic nuclear polarization (DNP) potentially offers significant...
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01-25-2014 02:07 PM
[NMR paper] Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-tc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy.
Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-tc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy.
Related Articles Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-tc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy.
Molecules. 2013;18(10):11904-11937
Authors: Ban D, Sabo TM, Griesinger C, Lee D
Abstract
Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics...
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10-01-2013 11:15 PM
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
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11-15-2011 10:36 AM
[KPWU blog] Some cartoon views of proteins shown in PyMOL
Some cartoon views of proteins shown in PyMOL
Example of cartoon modes of protein shown by PyMOL Example protein: 1UA8, LolA By default, the cartoon mode in PyMOL shows protein structure like this way: We can change the background to white by typing “bg_color white” in the command terminal and also change the color of protein based on types of secondary structures in http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=526&subd=kpwu&ref=&feed=1
Go to KPWU blog to read complete post.
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10-05-2011 08:52 AM
[NMR paper] Dynamic properties of proteins from NMR spectroscopy.
Dynamic properties of proteins from NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Dynamic properties of proteins from NMR spectroscopy.
Curr Opin Biotechnol. 1993 Aug;4(4):385-91
Authors: Palmer AG
Two-dimensional proton-detected heteronuclear nuclear magnetic resonance spectroscopy has been used to measure 13C and 15N spin-relaxation rate constants for several proteins. Generalized order parameters and effective internal correlation times have been...
New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy
Linear Mode
