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  Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques.

Rovo, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser, R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society, 141(2), 858-869. doi:10.1021/jacs.8b09258.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-BD7C-F Version Permalink: http://hdl.handle.net/21.11116/0000-0002-EC83-0
Genre: Journal Article

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Rovo, P., Author
Smith, C. A.1, Author              
Gauto, D., Author
de Groot, B. L.1, Author              
Schanda, P., Author
Linser, R., Author
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1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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 Abstract: NMR relaxation dispersion methods provide a holistic way to observe microsecond time-scale protein backbone motion both in solution and in the solid state. Different nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch-McConnell and near-rotary-resonance) give complementary information about the amplitudes and time scales of the conformational dynamics and provide comprehensive insights into the mechanistic details of the structural rearrangements. In this paper, we exemplify the benefits of the combination of various solution- and solid-state relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain), for which we are able to identify and model the functionally relevant conformational rearrangements around the ligand recognition loop occurring on multiple microsecond time scales. The observed loop motions suggest that the SH3 domain exists in a binding-competent conformation in dynamic equilibrium with a sterically impaired ground-state conformation both in solution and in crystalline form. This inherent plasticity between the interconverting macrostates is compatible with a conformational-preselection model and provides new insights into the recognition mechanisms of SH3 domains.

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Language(s): eng - English
 Dates: 2019-01-082019
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.8b09258
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 141 (2) Sequence Number: - Start / End Page: 858 - 869 Identifier: -