Mapping the population of protein confromational energy sub-states from NMR dipolar couplings.

Paul Guerry; Loic Salmon; Luca Mollica; Jose Luis Ortega Roldan; Phineus Markwick; Nico Van Nuland; Andrew Mccammon; Martin Blackledge

Mapping the population of protein confromational energy sub-states from NMR dipolar couplings.

Paul Guerry, Loic Salmon, Luca Mollica, Jose Luis Ortega Roldan, Phineus Markwick, Nico Van Nuland, Andrew Mccammon, Martin Blackledge

Department of Bio-engineering Sciences

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

42 Citations (Scopus)

Abstract

Molecular dynamics: A general method for the statistical mechanical description of conformational energy landscapes of proteins in solution is proposed. This method combines NMR residual dipolar couplings (RDCs), sampling of conformational space using accelerated molecular dynamics simulation, and ensemble selection using model-free ensemble interpretation of RDCs.

Original language	English
Pages (from-to)	3181-3185
Number of pages	5
Journal	Angewandte Chemie International Edition
Volume	52
Issue number	11
Publication status	Published - 11 Mar 2013

Keywords

NMR
RDC
protein dynamics

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http://onlinelibrary.wiley.com/doi/10.1002/anie.201209669/abstract;jsessionid=0029A9977D239A8D191480FAE1CFE015.d03t03

Cite this

Guerry, P., Salmon, L., Mollica, L., Ortega Roldan, J. L., Markwick, P., Van Nuland, N., Mccammon, A., & Blackledge, M. (2013). Mapping the population of protein confromational energy sub-states from NMR dipolar couplings. Angewandte Chemie International Edition, 52(11), 3181-3185. http://onlinelibrary.wiley.com/doi/10.1002/anie.201209669/abstract;jsessionid=0029A9977D239A8D191480FAE1CFE015.d03t03

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abstract = "Molecular dynamics: A general method for the statistical mechanical description of conformational energy landscapes of proteins in solution is proposed. This method combines NMR residual dipolar couplings (RDCs), sampling of conformational space using accelerated molecular dynamics simulation, and ensemble selection using model-free ensemble interpretation of RDCs.",

keywords = "NMR, RDC, protein dynamics",

author = "Paul Guerry and Loic Salmon and Luca Mollica and {Ortega Roldan}, {Jose Luis} and Phineus Markwick and {Van Nuland}, Nico and Andrew Mccammon and Martin Blackledge",

year = "2013",

month = mar,

day = "11",

language = "English",

volume = "52",

pages = "3181--3185",

journal = "Angewandte Chemie International Edition",

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Guerry, P, Salmon, L, Mollica, L, Ortega Roldan, JL, Markwick, P, Van Nuland, N, Mccammon, A & Blackledge, M 2013, 'Mapping the population of protein confromational energy sub-states from NMR dipolar couplings.', Angewandte Chemie International Edition, vol. 52, no. 11, pp. 3181-3185. <http://onlinelibrary.wiley.com/doi/10.1002/anie.201209669/abstract;jsessionid=0029A9977D239A8D191480FAE1CFE015.d03t03>

Mapping the population of protein confromational energy sub-states from NMR dipolar couplings. / Guerry, Paul; Salmon, Loic; Mollica, Luca; Ortega Roldan, Jose Luis; Markwick, Phineus; Van Nuland, Nico; Mccammon, Andrew; Blackledge, Martin.

In: Angewandte Chemie International Edition, Vol. 52, No. 11, 11.03.2013, p. 3181-3185.

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

TY - JOUR

T1 - Mapping the population of protein confromational energy sub-states from NMR dipolar couplings.

AU - Guerry, Paul

AU - Salmon, Loic

AU - Mollica, Luca

AU - Ortega Roldan, Jose Luis

AU - Markwick, Phineus

AU - Van Nuland, Nico

AU - Mccammon, Andrew

AU - Blackledge, Martin

PY - 2013/3/11

Y1 - 2013/3/11

N2 - Molecular dynamics: A general method for the statistical mechanical description of conformational energy landscapes of proteins in solution is proposed. This method combines NMR residual dipolar couplings (RDCs), sampling of conformational space using accelerated molecular dynamics simulation, and ensemble selection using model-free ensemble interpretation of RDCs.

AB - Molecular dynamics: A general method for the statistical mechanical description of conformational energy landscapes of proteins in solution is proposed. This method combines NMR residual dipolar couplings (RDCs), sampling of conformational space using accelerated molecular dynamics simulation, and ensemble selection using model-free ensemble interpretation of RDCs.

KW - NMR

KW - RDC

KW - protein dynamics

M3 - Article

VL - 52

SP - 3181

EP - 3185

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

SN - 1433-7851

IS - 11

ER -

Mapping the population of protein confromational energy sub-states from NMR dipolar couplings.

Abstract

Keywords

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