Automated analysis of NMR assignments and structures for proteins

H N Moseley; G T Montelione

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

Automated analysis of NMR assignments and structures for proteins

Curr Opin Struct Biol. 1999 Oct;9(5):635-42. doi: 10.1016/s0959-440x(99)00019-6.

Authors

H N Moseley¹, G T Montelione

Affiliation

¹ Center for Advanced Biotechnology and Medicine Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey, 08854-5638, USA. [email protected]

PMID: 10508776
DOI: 10.1016/s0959-440x(99)00019-6

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.

Publication types

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

MeSH terms

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

Substances

Proteins
Fibroblast Growth Factor 2

Grants and funding

GM-47014/GM/NIGMS NIH HHS/United States