Protein structures from NMR

In the last few years it has become possible to determine the three-dimensional structure of small proteins in solution by NMR methods. This is mainly due to advances in NMR technology such as the development of high-field spectrometers and new two-dimensional (2D) NMR techniques. Progress has also...

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Bibliographic Details
Published in:Biochemistry (Easton) 1988-07, Vol.27 (15), p.5389-5395
Main Authors: Kaptein, R, Boelens, R, Scheek, R. M, Van Gunsteren, W. F
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Computer Simulation
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Magnetic Resonance Spectroscopy - methods
Protein Conformation
Proteins
Repressor Proteins
reviews
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Summary:In the last few years it has become possible to determine the three-dimensional structure of small proteins in solution by NMR methods. This is mainly due to advances in NMR technology such as the development of high-field spectrometers and new two-dimensional (2D) NMR techniques. Progress has also been made to overcome the main bottleneck in the structure analysis of a protein, i.e., the assignment of super(1)H resonances. Finally, methods have been developed for structure determination on the basis of distance constraints from NMR such as distance geometry and restrained molecular dynamics. As a result, the structures of about 10 proteins, for which no crystallographic data were previously available, have now been determined by NMR. The authors will review the methods for protein structure determination on the basis of high-resolution NMR data.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00415a001