Local knowledge helps determine protein structures.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 105 ·No. 12 ·2008-03-25 ·Pages 4533-4

Gryk MR, Hoch JC

Abstract

暂无摘要

MeSH Terms

Magnetic Resonance Spectroscopy Models, Molecular Proteins/chemistry Software

Chemicals

Proteins

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Gryk Michael R

Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030-3305, USA.

Hoch Jeffrey C

References (12)

12 references, click to expand

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Use of chemical shifts in macromolecular structure determination.
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New methods of structure refinement for macromolecular structure determination by NMR.
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures.
Nature. 1992 Jan 30;355(6359):472-5 PMID: 18481394
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A comparison of quantum chemical models for calculating NMR shielding parameters in peptides: mixed basis set and ONIOM methods combined with a complete basis set extrapolation.
J Comput Chem. 2006 May;27(7):825-36 PMID: 16541428
Consistent blind protein structure generation from NMR chemical shift data.
Proc Natl Acad Sci U S A. 2008 Mar 25;105(12):4685-90 PMID: 18326625
Application of the random coil index to studying protein flexibility.
J Biomol NMR. 2008 Jan;40(1):31-48 PMID: 17985196
Protein backbone angle restraints from searching a database for chemical shift and sequence homology.
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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

1091-6490

DOI

10.1073/pnas.0801069105

Published

2008-03-25

Epub

2008-00-19

Pages

4533-4

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC2290792

Subset

Corrections

CommentOn

PMID: 18326625

External Links

PubMed source DOI: 10.1073/pnas.0801069105 PMC Full Text View journal details

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