Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings

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Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings. / Skrynnikov, N. R.; Kay, L. E.

в: Journal of Biomolecular NMR, Том 18, № 3, 2000, стр. 239-252.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

BibTeX

@article{301ccb35423f4af1afa3e20d7ea63028,

title = "Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings",

abstract = "Residual dipolar couplings measured in weakly aligning liquid-crystalline solvent contain valuable information on the structure of biomolecules in solution. Here we demonstrate that dipolar couplings (DCs) can be used to derive a comprehensive set of pairwise angular restraints that do not depend on the orientation of the alignment tensor principal axes. These restraints can be used to assess the agreement between a trial protein structure and a set of experimental dipolar couplings by means of a graphic representation termed a 'DC consistency map'. Importantly, these maps can be used to recognize structural elements consistent with the experimental DC data and to identify structural parameters that require further refinement, which could prove important for the success of DC-based structure calculations. This approach is illustrated for the 42 kDa maltodextrin-binding protein.",

keywords = "Alignment tensor, Domain orientation, Maltodextrin-binding protein, Orientational restraints, Protein structure, Residual dipolar couplings",

author = "Skrynnikov, {N. R.} and Kay, {L. E.}",

note = "Funding Information: We would like to thank Daiwen Yang for sharing with us his experimental data, Geofffrey Mueller for providing NOE-based structures prior to publication, Wing-Yiu Choy for help with software, and Natalie Goto for a critical reading of the manuscript. This work was supported by the Natural Sciences and Engineering Research Council of Canada and the Medical Research Council of Canada. N.R.S. acknowledges a postdoctoral scholarship from Le Fonds pour la Formation de Chercheurs et l{\textquoteright}Aide {\`a} la Recherche, Quebec. L.E.K. is a foreign investigator of the Howard Hughes Medical Research Institute. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.",

year = "2000",

doi = "10.1023/A:1026501101716",

language = "English",

volume = "18",

pages = "239--252",

journal = "Journal of Biomolecular NMR",

issn = "0925-2738",

publisher = "Springer Nature",

number = "3",

}

RIS

TY - JOUR

T1 - Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings

AU - Skrynnikov, N. R.

AU - Kay, L. E.

N1 - Funding Information: We would like to thank Daiwen Yang for sharing with us his experimental data, Geofffrey Mueller for providing NOE-based structures prior to publication, Wing-Yiu Choy for help with software, and Natalie Goto for a critical reading of the manuscript. This work was supported by the Natural Sciences and Engineering Research Council of Canada and the Medical Research Council of Canada. N.R.S. acknowledges a postdoctoral scholarship from Le Fonds pour la Formation de Chercheurs et l’Aide à la Recherche, Quebec. L.E.K. is a foreign investigator of the Howard Hughes Medical Research Institute. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.

PY - 2000

Y1 - 2000

N2 - Residual dipolar couplings measured in weakly aligning liquid-crystalline solvent contain valuable information on the structure of biomolecules in solution. Here we demonstrate that dipolar couplings (DCs) can be used to derive a comprehensive set of pairwise angular restraints that do not depend on the orientation of the alignment tensor principal axes. These restraints can be used to assess the agreement between a trial protein structure and a set of experimental dipolar couplings by means of a graphic representation termed a 'DC consistency map'. Importantly, these maps can be used to recognize structural elements consistent with the experimental DC data and to identify structural parameters that require further refinement, which could prove important for the success of DC-based structure calculations. This approach is illustrated for the 42 kDa maltodextrin-binding protein.

AB - Residual dipolar couplings measured in weakly aligning liquid-crystalline solvent contain valuable information on the structure of biomolecules in solution. Here we demonstrate that dipolar couplings (DCs) can be used to derive a comprehensive set of pairwise angular restraints that do not depend on the orientation of the alignment tensor principal axes. These restraints can be used to assess the agreement between a trial protein structure and a set of experimental dipolar couplings by means of a graphic representation termed a 'DC consistency map'. Importantly, these maps can be used to recognize structural elements consistent with the experimental DC data and to identify structural parameters that require further refinement, which could prove important for the success of DC-based structure calculations. This approach is illustrated for the 42 kDa maltodextrin-binding protein.

KW - Alignment tensor

KW - Domain orientation

KW - Maltodextrin-binding protein

KW - Orientational restraints

KW - Protein structure

KW - Residual dipolar couplings

UR - http://www.scopus.com/inward/record.url?scp=0033636451&partnerID=8YFLogxK

U2 - 10.1023/A:1026501101716

DO - 10.1023/A:1026501101716

M3 - Article

C2 - 11142514

VL - 18

SP - 239

EP - 252

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

SN - 0925-2738

IS - 3

ER -

ID: 74231156