Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin

Loïe Salmon; Guillaume Bouvignies; Phineus Markwick; Nils Lakomek; Scott Showalter; Da Wei Li; Korvin Walter; Christian Griesinger; Rafael Brüschweiler; Martin Blackledge

doi:10.1002/anie.200900476

Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin

Loïe Salmon
, Guillaume Bouvignies
, Phineus Markwick
, Nils Lakomek
, Scott Showalter
, Da Wei Li
, Korvin Walter
, Christian Griesinger
, Rafael Brüschweiler
, Martin Blackledge

Research output: Contribution to journal › Article › peer-review

79 Scopus citations

Abstract

A robust procedure for the determination of proteinbackbone motions on time scales of pico- to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular-dynamics trajectory of ubiquitin (red).

Original language	English (US)
Pages (from-to)	4154-4157
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	23
DOIs	https://doi.org/10.1002/anie.200900476
State	Published - May 25 2009

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry

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10.1002/anie.200900476

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Salmon, L., Bouvignies, G., Markwick, P., Lakomek, N., Showalter, S., Li, D. W., Walter, K., Griesinger, C., Brüschweiler, R., & Blackledge, M. (2009). Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin. Angewandte Chemie - International Edition, 48(23), 4154-4157. https://doi.org/10.1002/anie.200900476

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abstract = "A robust procedure for the determination of proteinbackbone motions on time scales of pico- to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular-dynamics trajectory of ubiquitin (red).",

author = "Lo{\"i}e Salmon and Guillaume Bouvignies and Phineus Markwick and Nils Lakomek and Scott Showalter and Li, \{Da Wei\} and Korvin Walter and Christian Griesinger and Rafael Br{\"u}schweiler and Martin Blackledge",

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Salmon, L, Bouvignies, G, Markwick, P, Lakomek, N, Showalter, S, Li, DW, Walter, K, Griesinger, C, Brüschweiler, R & Blackledge, M 2009, 'Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin', Angewandte Chemie - International Edition, vol. 48, no. 23, pp. 4154-4157. https://doi.org/10.1002/anie.200900476

Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin. / Salmon, Loïe; Bouvignies, Guillaume; Markwick, Phineus et al.
In: Angewandte Chemie - International Edition, Vol. 48, No. 23, 25.05.2009, p. 4154-4157.

Research output: Contribution to journal › Article › peer-review

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AU - Salmon, Loïe

AU - Bouvignies, Guillaume

AU - Markwick, Phineus

AU - Lakomek, Nils

AU - Showalter, Scott

AU - Li, Da Wei

AU - Walter, Korvin

AU - Griesinger, Christian

AU - Brüschweiler, Rafael

AU - Blackledge, Martin

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AB - A robust procedure for the determination of proteinbackbone motions on time scales of pico- to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular-dynamics trajectory of ubiquitin (red).

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JF - Angewandte Chemie - International Edition

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Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin

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