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PMID: 9470228 Published · ppublish English Journal Article Review

Determining the structures of large proteins and protein complexes by NMR.

Trends in biotechnology ·Vol. 16 ·No. 1 ·1998-01-00 ·Pages 22-34

Clore GM, Gronenborn AM

Abstract

Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess of 250 residues to be solved. These developments may permit the determination by NMR of the structures of macromolecules up to 50-60kDa, thereby bringing into reach numerous systems of considerable biological interest, including a large variety of protein-protein and protein-nucleic-acid complexes.

MeSH Terms
Magnetic Resonance Spectroscopy Protein Conformation
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Clore G M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Healthy, Bethesda, MD 20892-0520, USA.
Gronenborn A M
Article Info
Journal
Trends in biotechnology
Abbr.
Trends Biotechnol
ISSN
0167-7799
Published
1998-01-00
Pages
22-34
Language
English
Region
England
NLM ID
8310903
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