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Characterization of protein–protein interfaces in large complexes by solid-state NMR solvent paramagnetic relaxation enhancements

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Öster, Carl, Kosol, Simone, Hartmüller, Christoph, Lamley, Jonathan M., Iuga, Dinu, Oss, Andres, Org, Mai-Liis, Vanatalu, Kalju, Samoson, Ago, Madl, Tobias and Lewandowski, Józef R. (2017) Characterization of protein–protein interfaces in large complexes by solid-state NMR solvent paramagnetic relaxation enhancements. Journal of the American Chemical Society, 139 (35). pp. 12165-12174. doi:10.1021/jacs.7b03875 ISSN 0002-7863.

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Official URL: http://pubs.acs.org/doi/10.1021/jacs.7b03875

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Abstract

Solid-state NMR is becoming a viable alternative for obtaining information about structures and dynamics of large biomolecular complexes, including ones that are not accessible to other high-resolution biophysical techniques. In this context, methods for probing protein−protein interfaces at atomic resolution are highly desirable. Solvent paramagnetic relaxation enhancements (sPREs) proved to be a powerful method for probing protein−protein interfaces in large complexes in solution but have not been employed toward this goal in the solid state. We demonstrate that 1H and 15N relaxation-based sPREs provide a powerful tool for characterizing intermolecular interactions in large assemblies in the solid state. We present approaches for measuring sPREs in practically the entire range of magic angle spinning frequencies used for biomolecular studies and discuss their benefits and limitations. We validate the approach on crystalline GB1, with our experimental results in good agreement with theoretical predictions. Finally, we use sPREs to characterize protein−protein interfaces in the GB1 complex with immunoglobulin G (IgG). Our results suggest the potential existence of an additional binding site and provide new insights into GB1:IgG complex structure that amend and revise the current model available from studies with IgG fragments. We demonstrate sPREs as a practical, widely applicable, robust, and very sensitive technique for determining intermolecular interaction interfaces in large biomolecular complexes in the solid state.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH): Protein-protein interactions, Nuclear magnetic resonance spectroscopy
Journal or Publication Title: Journal of the American Chemical Society
Publisher: American Chemical Society
ISSN: 0002-7863
Official Date: 6 September 2017
Dates:
DateEvent
6 September 2017Published
7 August 2017Available
6 August 2017Accepted
Volume: 139
Number: 35
Page Range: pp. 12165-12174
DOI: 10.1021/jacs.7b03875
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 25 August 2017
Date of first compliant Open Access: 29 August 2017
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
(FP/2007-2013)/ERC Grant Agreement 639907Seventh Framework Programmehttp://dx.doi.org/10.13039/100011102
RG130022 Royal Societyhttp://dx.doi.org/10.13039/501100000288
EP/L025906/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
BB/L022761/1Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
OPP1160394Bill and Melinda Gates Foundationhttp://dx.doi.org/10.13039/100000865
316630 CAS-IDPSeventh Framework Programmehttp://dx.doi.org/10.13039/100011102
BB/L022761/1 Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
UNSPECIFIEDOmicsCenter GrazUNSPECIFIED
UNSPECIFIEDBayerisches Staatsministerium für Wissenschaft, Forschung und Kunsthttp://dx.doi.org/10.13039/501100005341
2015VBB045Chinese Academy of Scienceshttp://dx.doi.org/10.13039/501100002367
31450110423National Natural Science Foundation of Chinahttp://dx.doi.org/10.13039/501100001809
FWF: P28854, W1226-B18Austrian Science Fundhttp://dx.doi.org/10.13039/501100002428
DFG, MA5703/1-1Deutsche Forschungsgemeinschafthttp://dx.doi.org/10.13039/501100001659
Austrian infrastructure program 2016/2017, BioTechMed/GrazIntegrative Metabolism Research Center GrazUNSPECIFIED
PR140003[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
PR140003Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
UNSPECIFIEDUniversity of Warwickhttp://dx.doi.org/10.13039/501100000741
UNSPECIFIEDBirmingham Science CityUNSPECIFIED
UNSPECIFIEDAdvantage West Midlands (AWM)UNSPECIFIED
UNSPECIFIEDEuropean Regional Development Fundhttp://dx.doi.org/10.13039/501100008530
PUT 1534Eesti Teadusagentuurhttp://dx.doi.org/10.13039/501100002301
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