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PMID: 10508776 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Automated analysis of NMR assignments and structures for proteins.

Current opinion in structural biology ·Vol. 9 ·No. 5 ·1999-10-00 ·Pages 635-42

Moseley HN, Montelione GT

Abstract

Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.

MeSH Terms

Automation/methods Fibroblast Growth Factor 2/chemistry Models, Molecular Nuclear Magnetic Resonance, Biomolecular/methods Protein Conformation Protein Structure, Secondary Proteins/chemistry

Chemicals

Proteins Fibroblast Growth Factor 2

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Moseley H N

Center for Advanced Biotechnology and Medicine Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey, 08854-5638, USA. hunter@cabm.rutgers.edu

Montelione G T

Article Info

Journal

Current opinion in structural biology

Abbr.

Curr Opin Struct Biol

ISSN

0959-440X

DOI

10.1016/s0959-440x(99)00019-6

hunter@cabm.rutgers.edu

Published

1999-10-00

Pages

635-42

Language

English

Region

England

NLM ID

9107784

Subset

Grants

NIGMS NIH HHS · GM-47014 · United States

External Links

PubMed source DOI: 10.1016/s0959-440x(99)00019-6 View journal details

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Automated analysis of NMR assignments and structures for proteins.

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