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The Exact Nuclear Overhauser Enhancement: Recent Advances.
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2017 (English)In: Molecules, ISSN 1420-3049, E-ISSN 1420-3049, Vol. 22, no 7, E1176Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2017. Vol. 22, no 7, E1176
Keyword [en]
NMR, allostery, biological macromolecules, conformational space, correlated dynamics, dynamics, exact NOE, proteins, structure calculation, structure ensemble
Identifiers
URN: urn:nbn:se:uu:diva-331630DOI: 10.3390/molecules22071176PubMedID: 28708092OAI: oai:DiVA.org:uu-331630DiVA: diva2:1149523
Available from: 2017-10-16 Created: 2017-10-16 Last updated: 2017-10-16

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Chi N, Celestine
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Department of Medical Biochemistry and Microbiology
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