Abstract
Solid-state NMR spectroscopy proved to be a versatile tool for characterization of structure and dynamics of complex biochemical systems. In particular, magic angle spinning (MAS) solid-state NMR came to maturity for application towards structural elucidation of biological macromolecules. Current challenges in applying solid-state NMR as well as progress achieved recently will be discussed in the following chapter focusing on conceptual aspects important for structural elucidation of proteins.
PMID: 23504090 [PubMed - as supplied by publisher]
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Abstract Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the...
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09-20-2012 06:06 AM
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Martin Tollinger, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst and Paul Schanda
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303591y/aop/images/medium/ja-2012-03591y_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303591y
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http://feeds.feedburner.com/~r/acs/jacsat/~4/ZVmFwVkbuRs
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08-29-2012 04:28 AM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 20;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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04-22-2011 02:00 PM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 14;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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04-16-2011 12:29 PM
Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy
Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy
Abstract We present a systematic study of the effect of the level of exchangeable protons on the observed amide proton linewidth obtained in perdeuterated proteins. Decreasing the amount of D2O employed in the crystallization buffer from 90 to 0%, we observe a fourfold increase in linewidth for both 1H and 15N resonances. At the same time, we find a gradual increase in the signal-to-noise ratio (SNR) for 1Hâ??15N correlations in dipolar coupling based experiments for...
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01-09-2011 12:46 PM
[NMR paper] Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins u
Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
Related Articles Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
J Am Chem Soc. 2003 Oct 1;125(39):11816-7
Authors: Duma L, Hediger S, Brutscher B, Böckmann A, Emsley L
We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer...
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11-24-2010 09:16 PM
[NMR paper] Solid-state NMR spectroscopy applied to membrane proteins.
Solid-state NMR spectroscopy applied to membrane proteins.
Related Articles Solid-state NMR spectroscopy applied to membrane proteins.
Curr Opin Struct Biol. 2000 Oct;10(5):593-600
Authors: de Groot HJ
One major remaining problem in structural biology is to elucidate the structure and mechanism of function of membrane proteins. On the basis of preliminary information from genome projects, it is now estimated that up to 50,000 different membrane proteins may exist in the human being and that virtually every life process proceeds, sooner or...
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11-19-2010 08:29 PM
GFT projection NMR spectroscopy for proteins in the solid state.
GFT projection NMR spectroscopy for proteins in the solid state.
GFT projection NMR spectroscopy for proteins in the solid state.
J Biomol NMR. 2010 Oct 30;
Authors: Trent Franks W, Atreya HS, Szyperski T, Rienstra CM
Recording of four-dimensional (4D) spectra for proteins in the solid state has opened new avenues to obtain virtually complete resonance assignments and three-dimensional (3D) structures of proteins. As in solution state NMR, the sampling of three indirect dimensions leads per se to long minimal measurement time. Furthermore,...
Solid-State NMR Spectroscopy of Proteins.
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