Computational methods for determining protein structures from NMR data

Garry P. Gippert; Ping F. Yip; Peter E. Wright; David A. Case

doi:10.1016/0006-2952(90)90172-H

Computational methods for determining protein structures from NMR data

Garry P. Gippert, Ping F. Yip, Peter E. Wright, David A. Case

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

69 Scopus citations

Abstract

The general procedures by which solution structures of proteins may be deduced from distance and angular constraints derived from NMR are reviewed, with an emphasis on practical aspects of the calculations. In addition, novel methods based on chemical shift calculations and on quantitative fits to nuclear Overhauser effect intensities are presented; these should provide improved understanding of the limits of our ability to simulate complex spectra, and may permit higher precision structures to be determined.

Original language	English (US)
Pages (from-to)	15-22
Number of pages	8
Journal	Biochemical Pharmacology
Volume	40
Issue number	1
DOIs	https://doi.org/10.1016/0006-2952(90)90172-H
State	Published - Jul 1 1990
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Pharmacology

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10.1016/0006-2952(90)90172-H

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title = "Computational methods for determining protein structures from NMR data",

abstract = "The general procedures by which solution structures of proteins may be deduced from distance and angular constraints derived from NMR are reviewed, with an emphasis on practical aspects of the calculations. In addition, novel methods based on chemical shift calculations and on quantitative fits to nuclear Overhauser effect intensities are presented; these should provide improved understanding of the limits of our ability to simulate complex spectra, and may permit higher precision structures to be determined.",

author = "Gippert, {Garry P.} and Yip, {Ping F.} and Wright, {Peter E.} and Case, {David A.}",

note = "Funding Information: Acknowledgements-We thank Jane Dyson, Jonathan Moore and Walter Chazin for helpful discussions.T his work wass upportedi n part by NIH Grants GM 38794a nd GM 36643.",

year = "1990",

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doi = "10.1016/0006-2952(90)90172-H",

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T1 - Computational methods for determining protein structures from NMR data

AU - Gippert, Garry P.

AU - Yip, Ping F.

AU - Wright, Peter E.

AU - Case, David A.

N1 - Funding Information: Acknowledgements-We thank Jane Dyson, Jonathan Moore and Walter Chazin for helpful discussions.T his work wass upportedi n part by NIH Grants GM 38794a nd GM 36643.

PY - 1990/7/1

Y1 - 1990/7/1

N2 - The general procedures by which solution structures of proteins may be deduced from distance and angular constraints derived from NMR are reviewed, with an emphasis on practical aspects of the calculations. In addition, novel methods based on chemical shift calculations and on quantitative fits to nuclear Overhauser effect intensities are presented; these should provide improved understanding of the limits of our ability to simulate complex spectra, and may permit higher precision structures to be determined.

AB - The general procedures by which solution structures of proteins may be deduced from distance and angular constraints derived from NMR are reviewed, with an emphasis on practical aspects of the calculations. In addition, novel methods based on chemical shift calculations and on quantitative fits to nuclear Overhauser effect intensities are presented; these should provide improved understanding of the limits of our ability to simulate complex spectra, and may permit higher precision structures to be determined.

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U2 - 10.1016/0006-2952(90)90172-H

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JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

IS - 1

ER -

Computational methods for determining protein structures from NMR data

Abstract

All Science Journal Classification (ASJC) codes

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