Next Article in Journal
Cholinesterase and Prolyl Oligopeptidase Inhibitory Activities of Alkaloids from Argemone platyceras (Papaveraceae)
Next Article in Special Issue
Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA
Previous Article in Journal
Metal-Free Regiodivergent Addition of Carbon Nucleophiles to α,β-Unsaturated Electrophiles
Previous Article in Special Issue
Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1
Article Menu
Issue 7 (July) cover image

Export Article

Open AccessFeature PaperReview
Molecules 2017, 22(7), 1176;

The Exact Nuclear Overhauser Enhancement: Recent Advances

Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA
Faculty of Pharmacy, Mansoura University, Mansoura 35516, Egypt
Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich 8093, Switzerland
Department of Mathematics and Computer Science, Freie Universität Berlin, Arnimallee 6, Berlin 14195, Germany
Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Frankfurt am Main 60438, Germany
Graduate School of Science, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan
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)
Full-Text   |   PDF [7235 KB, uploaded 14 July 2017]   |  


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

Graphical abstract

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).

Share & Cite This Article

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top