Site-specific variations of carbonyl chemical shift anisotropies in proteins.

Site-specific variations of carbonyl chemical shift anisotropies in proteins. Research Abstract Details 

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Site-specific variations of carbonyl chemical shift anisotropies in proteins. Abstract Text:

Phineus R L Markwick,Michael Sattler,

By combining molecular dynamics (MD) simulation with a novel extended density functional theory method, we calculate site-specific carbonyl chemical shift tensors in the SMN Tudor domain. We formulate a simple model for the C' chemical shift anisotropy (CSA) based solely on the isotropic chemical shift. Using this simple chemical shift tensor model and the MD simulation, an accurate prediction of transverse C'/N-H cross-correlated relaxation rates can be obtained.

Site-specific variations of carbonyl chemical shift anisotropies in proteins. Publishing Authors By Initials

PR Markwick,M Sattler,

For similar proteins research abstracts see: proteins research

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Site-specific variations of carbonyl chemical shift anisotropies in proteins. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Chemical Society

VOLUME: 126

Page Numbers: 11424-5

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 22

MONTH: Sep

YEAR: 2004

Site-specific variations of carbonyl chemical shift anisotropies in proteins. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Site-specific variations of carbonyl chemical shift anisotropies in proteins. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: chemistry

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Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for Site-specific variations of carbonyl chemical shift anisotropies in proteins.

AFFILIATION: EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

Country: United States

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MEDLINETA: J Am Chem Soc

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