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Molecules 2017, 22(7), 1176; doi:10.3390/molecules22071176

The Exact Nuclear Overhauser Enhancement: Recent Advances

1
Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA
2
Faculty of Pharmacy, Mansoura University, Mansoura 35516, Egypt
3
Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich 8093, Switzerland
4
Department of Mathematics and Computer Science, Freie Universität Berlin, Arnimallee 6, Berlin 14195, Germany
5
Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Frankfurt am Main 60438, Germany
6
Graduate School of Science, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan
7
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, Uppsala SE-75123, Sweden
*
Author to whom correspondence should be addressed.
Academic Editors: Chojiro Kojima, Shang-Te Danny Hsu and Bong-Jin Lee
Received: 22 June 2017 / Accepted: 10 July 2017 / Published: 14 July 2017
(This article belongs to the Special Issue Recent Advances in Biomolecular NMR Spectroscopy)
View Full-Text   |   Download PDF [7235 KB, uploaded 14 July 2017]   |  

Abstract

Although often depicted as rigid structures, proteins are highly dynamic systems, whose motions are essential to their functions. Despite this, it is difficult to investigate protein dynamics due to the rapid timescale at which they sample their conformational space, leading most NMR-determined structures to represent only an averaged snapshot of the dynamic picture. While NMR relaxation measurements can help to determine local dynamics, it is difficult to detect translational or concerted motion, and only recently have significant advances been made to make it possible to acquire a more holistic representation of the dynamics and structural landscapes of proteins. Here, we briefly revisit our most recent progress in the theory and use of exact nuclear Overhauser enhancements (eNOEs) for the calculation of structural ensembles that describe their conformational space. New developments are primarily targeted at increasing the number and improving the quality of extracted eNOE distance restraints, such that the multi-state structure calculation can be applied to proteins of higher molecular weights. We then review the implications of the exact NOE to the protein dynamics and function of cyclophilin A and the WW domain of Pin1, and finally discuss our current research and future directions. View Full-Text
Keywords: NMR; biological macromolecules; proteins; dynamics; correlated dynamics; exact NOE; structure calculation; structure ensemble; allostery; conformational space NMR; biological macromolecules; proteins; dynamics; correlated dynamics; exact NOE; structure calculation; structure ensemble; allostery; conformational space
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Nichols, P.J.; Born, A.; Henen, M.A.; Strotz, D.; Orts, J.; Olsson, S.; Güntert, P.; Chi, C.N.; Vögeli, B. The Exact Nuclear Overhauser Enhancement: Recent Advances. Molecules 2017, 22, 1176.

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