[NMR paper] Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-tc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy.
Related ArticlesMeasuring 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 and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-tc window (defined as tc < supra-tc < 40 ms; in which tc is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-tc window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-tc scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-tc scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-tc scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.
PMID: 24077173 [PubMed - as supplied by publisher]
[NMR paper] Solid-State NMR Approaches to Internal Dynamics of Proteins: From Picoseconds to Microseconds and Seconds.
Solid-State NMR Approaches to Internal Dynamics of Proteins: From Picoseconds to Microseconds and Seconds.
Solid-State NMR Approaches to Internal Dynamics of Proteins: From Picoseconds to Microseconds and Seconds.
Acc Chem Res. 2013 Jul 23;
Authors: Krushelnitsky A, Reichert D, Saalwächter K
Abstract
Solid-state nuclear magnetic resonance (NMR) spectroscopy has matured to the point that it is possible to determine the structure of proteins in immobilized states, such as within microcrystals or embedded in membranes. Currently, researchers...
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07-24-2013 04:52 PM
Continuously Tunable 250 GHz Gyrotron with a Double Disk Window for DNP-NMR Spectroscopy
From The DNP-NMR Blog:
Continuously Tunable 250 GHz Gyrotron with a Double Disk Window for DNP-NMR Spectroscopy
Jawla, S., et al., Continuously Tunable 250 GHz Gyrotron with a Double Disk Window for DNP-NMR Spectroscopy. J Infrared Milli Terahz Waves, 2013. 34(1): p. 42-52.
http://dx.doi.org/10.1007/s10762-012-9947-1
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04-24-2013 09:48 PM
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.
J Magn Reson. 2011 Mar 30;
Authors: Kay LE
With the development of appropriate labeling schemes and the associated experiments that exploit them it has become possible to record high quality solution NMR spectra of supra-molecular complexes with molecular masses extending to 1MDa. One such approach involves selective (13)CH(3) methyl labeling in highly deuterated proteins...
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04-05-2011 10:22 PM
Solution NMR Spectroscopy of Supra-Molecular Systems, Why Bother? A Methyl TROSY View
Solution NMR Spectroscopy of Supra-Molecular Systems, Why Bother? A Methyl TROSY View
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 8 March 2011</br>
Lewis E., Kay</br>
With the development of appropriate labeling schemes and the associated experiments that exploit them it has become possible to record high quality solution NMR spectra of supra-molecular complexes with molecular masses extending to 1MDa. One such approach involves selective 13CH3 methyl labeling in highly deuterated proteins using experiments that make...
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[NMR paper] Real-time NMR kinetic studies provide global and residue-specific information on the
Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
Related Articles Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
J Mol Biol. 2003 May 2;328(3):693-703
Authors: Roy M, Jennings PA
The interleukin-1beta (IL-1beta) structural motif is a beta-trefoil super fold created by six two-stranded beta-hairpins. Turns are thus...
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11-24-2010 09:01 PM
[NMR paper] A novel approach to the retrieval of structural and dynamic information from residual
A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy.
Related Articles A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy.
J Am Chem Soc. 2002 Oct 9;124(40):12020-30
Authors: Tolman JR
The interpretation of residual dipolar couplings in terms of molecular properties of interest is complicated because of difficulties in...
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11-24-2010 08:58 PM
[NMR paper] Kinetic studies of protein folding using NMR spectroscopy.
Kinetic studies of protein folding using NMR spectroscopy.
Related Articles Kinetic studies of protein folding using NMR spectroscopy.
Nat Struct Biol. 1998 Jul;5 Suppl:504-7
Authors: Dobson CM, Hore PJ
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[NMR paper] Exploring the dynamic information content of a protein NMR structure: comparison of a
Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
Proteins. 1999 Jul 1;36(1):87-110
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Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-tc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy.
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