Molecular dynamics and NMR spin relaxation in proteins

David A. Case

doi:https://doi.org/10.1021/ar010020l

Molecular dynamics and NMR spin relaxation in proteins

David A. Case

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

167 Scopus citations

Abstract

Molecular dynamics simulations often play a central role in the analysis of biomolecular NMR data. The focus here is on NMR spin-relaxation, which can provide unique insights into the time-dependence of conformational fluctuations, especially on picosecond to nanosecond time scales which can be directly probed by simulations. A great deal has been learned from such simulations about the general nature of such motions and their impact on NMR observables. In principle, relaxation measurements should also provide valuable benchmarks for judging the quantitative accuracy of simulations, but there are a variety of experimental and computational obstacles to making useful direct comparisons. It seems likely that simulations on time scales that are just now becoming generally feasible may provide important new information on internal motions, overall rotational diffusion, and the coupling between internal and rotational motion. Such information could provide a sound foundation for a new generation of detailed interpretation of NMR spin-relaxation results.

Original language	English (US)
Pages (from-to)	325-331
Number of pages	7
Journal	Accounts of Chemical Research
Volume	35
Issue number	6
DOIs	https://doi.org/10.1021/ar010020l
State	Published - 2002
Externally published	Yes

ASJC Scopus subject areas

Chemistry(all)

Access to Document

https://doi.org/10.1021/ar010020l

Cite this

@article{ecfa7f2587a340719ceaf113cccce2de,

title = "Molecular dynamics and NMR spin relaxation in proteins",

abstract = "Molecular dynamics simulations often play a central role in the analysis of biomolecular NMR data. The focus here is on NMR spin-relaxation, which can provide unique insights into the time-dependence of conformational fluctuations, especially on picosecond to nanosecond time scales which can be directly probed by simulations. A great deal has been learned from such simulations about the general nature of such motions and their impact on NMR observables. In principle, relaxation measurements should also provide valuable benchmarks for judging the quantitative accuracy of simulations, but there are a variety of experimental and computational obstacles to making useful direct comparisons. It seems likely that simulations on time scales that are just now becoming generally feasible may provide important new information on internal motions, overall rotational diffusion, and the coupling between internal and rotational motion. Such information could provide a sound foundation for a new generation of detailed interpretation of NMR spin-relaxation results.",

author = "Case, {David A.}",

year = "2002",

doi = "https://doi.org/10.1021/ar010020l",

language = "English (US)",

volume = "35",

pages = "325--331",

journal = "Accounts of Chemical Research",

issn = "0001-4842",

publisher = "American Chemical Society",

number = "6",

}

TY - JOUR

T1 - Molecular dynamics and NMR spin relaxation in proteins

AU - Case, David A.

PY - 2002

Y1 - 2002

N2 - Molecular dynamics simulations often play a central role in the analysis of biomolecular NMR data. The focus here is on NMR spin-relaxation, which can provide unique insights into the time-dependence of conformational fluctuations, especially on picosecond to nanosecond time scales which can be directly probed by simulations. A great deal has been learned from such simulations about the general nature of such motions and their impact on NMR observables. In principle, relaxation measurements should also provide valuable benchmarks for judging the quantitative accuracy of simulations, but there are a variety of experimental and computational obstacles to making useful direct comparisons. It seems likely that simulations on time scales that are just now becoming generally feasible may provide important new information on internal motions, overall rotational diffusion, and the coupling between internal and rotational motion. Such information could provide a sound foundation for a new generation of detailed interpretation of NMR spin-relaxation results.

AB - Molecular dynamics simulations often play a central role in the analysis of biomolecular NMR data. The focus here is on NMR spin-relaxation, which can provide unique insights into the time-dependence of conformational fluctuations, especially on picosecond to nanosecond time scales which can be directly probed by simulations. A great deal has been learned from such simulations about the general nature of such motions and their impact on NMR observables. In principle, relaxation measurements should also provide valuable benchmarks for judging the quantitative accuracy of simulations, but there are a variety of experimental and computational obstacles to making useful direct comparisons. It seems likely that simulations on time scales that are just now becoming generally feasible may provide important new information on internal motions, overall rotational diffusion, and the coupling between internal and rotational motion. Such information could provide a sound foundation for a new generation of detailed interpretation of NMR spin-relaxation results.

UR - http://www.scopus.com/inward/record.url?scp=0036283096&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036283096&partnerID=8YFLogxK

U2 - https://doi.org/10.1021/ar010020l

DO - https://doi.org/10.1021/ar010020l

M3 - Article

C2 - 12069616

VL - 35

SP - 325

EP - 331

JO - Accounts of Chemical Research

JF - Accounts of Chemical Research

SN - 0001-4842

IS - 6

ER -

Molecular dynamics and NMR spin relaxation in proteins

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this