A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment

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A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment. / Mueller, Geoffrey A.; Choy, W. Y.; Skrynnikov, Nikolai R.; Kay, Lewis E.

In: Journal of Biomolecular NMR, Vol. 18, No. 3, 2000, p. 183-188.

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

Author

Mueller, Geoffrey A. ; Choy, W. Y. ; Skrynnikov, Nikolai R. ; Kay, Lewis E. / A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment. In: Journal of Biomolecular NMR. 2000 ; Vol. 18, No. 3. pp. 183-188.

BibTeX

@article{a95963df40184c71a87dc23ae358d92d,

title = "A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment",

abstract = "A method for incorporating dipolar coupling restraints into structure calculations in described which follows closely on methodology that has been recently presented for orienting peptide planes using dipolar couplings [Mueller et al. (2000) J. Mol. Biol., 300, 197-212] and is specifically developed for use in cases of an axially symmetric alignment tensor. Modeling studies on an all α-helical protein, farnesyl diphosphate synthase, establish the utility of the approach. A global fold of the 370-residue maltose binding protein in complex with β-cyclodextrin is obtained from experimentally derived restraints. The average pairwise rmsd values between the N- and C-terminal domains in this NMR structure and the corresponding regions in the X-ray structure of the protein are 2.8 and 3.1 {\AA}, respectively.",

keywords = "Deuteration, High molecular weight proteins, Methyl protonation, Residual dipolar couplings",

author = "Mueller, {Geoffrey A.} and Choy, {W. Y.} and Skrynnikov, {Nikolai R.} and Kay, {Lewis E.}",

note = "Funding Information: G.A.M, W.Y.C and N.R.S are recipients of postdoctoral fellowships from the Human Frontiers Science Program, the Croucher Foundation and Le Fonds pour la Formation de Chercheurs et l{\textquoteright}Aide a la Recherche, Quebec, respectively. This work was supported by a grant from the Medical Research Council of Canada. L.E.K is an International Research Scholar of the Howard Hughes Medical Institute. All software developed is available from the authors upon request. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.",

year = "2000",

doi = "10.1023/A:1026788430236",

language = "English",

volume = "18",

pages = "183--188",

journal = "Journal of Biomolecular NMR",

issn = "0925-2738",

publisher = "Springer Nature",

number = "3",

}

RIS

TY - JOUR

T1 - A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment

AU - Mueller, Geoffrey A.

AU - Choy, W. Y.

AU - Skrynnikov, Nikolai R.

AU - Kay, Lewis E.

N1 - Funding Information: G.A.M, W.Y.C and N.R.S are recipients of postdoctoral fellowships from the Human Frontiers Science Program, the Croucher Foundation and Le Fonds pour la Formation de Chercheurs et l’Aide a la Recherche, Quebec, respectively. This work was supported by a grant from the Medical Research Council of Canada. L.E.K is an International Research Scholar of the Howard Hughes Medical Institute. All software developed is available from the authors upon request. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.

PY - 2000

Y1 - 2000

N2 - A method for incorporating dipolar coupling restraints into structure calculations in described which follows closely on methodology that has been recently presented for orienting peptide planes using dipolar couplings [Mueller et al. (2000) J. Mol. Biol., 300, 197-212] and is specifically developed for use in cases of an axially symmetric alignment tensor. Modeling studies on an all α-helical protein, farnesyl diphosphate synthase, establish the utility of the approach. A global fold of the 370-residue maltose binding protein in complex with β-cyclodextrin is obtained from experimentally derived restraints. The average pairwise rmsd values between the N- and C-terminal domains in this NMR structure and the corresponding regions in the X-ray structure of the protein are 2.8 and 3.1 Å, respectively.

AB - A method for incorporating dipolar coupling restraints into structure calculations in described which follows closely on methodology that has been recently presented for orienting peptide planes using dipolar couplings [Mueller et al. (2000) J. Mol. Biol., 300, 197-212] and is specifically developed for use in cases of an axially symmetric alignment tensor. Modeling studies on an all α-helical protein, farnesyl diphosphate synthase, establish the utility of the approach. A global fold of the 370-residue maltose binding protein in complex with β-cyclodextrin is obtained from experimentally derived restraints. The average pairwise rmsd values between the N- and C-terminal domains in this NMR structure and the corresponding regions in the X-ray structure of the protein are 2.8 and 3.1 Å, respectively.

KW - Deuteration

KW - High molecular weight proteins

KW - Methyl protonation

KW - Residual dipolar couplings

UR - http://www.scopus.com/inward/record.url?scp=0033637626&partnerID=8YFLogxK

U2 - 10.1023/A:1026788430236

DO - 10.1023/A:1026788430236

M3 - Article

C2 - 11142508

VL - 18

SP - 183

EP - 188

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

SN - 0925-2738

IS - 3

ER -

ID: 74232703