structural analysis of protein-protein interactions by NMR spectroscopy

A comprehensive understanding of protein-protein interactions is an important next step in our quest to understand how the information contained in a genome is put into action. Although a number of experimental techniques can report on the existence of a protein- protein interaction, very few can pr...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2009-12, Vol.9 (23), p.5224-5232
Main Authors: O'Connell, Mitchell R, Gamsjaeger, Roland, Mackay, Joel P
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Humans
Miscellaneous
Models, Molecular
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - instrumentation
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Conformation
Protein Interaction Mapping - instrumentation
Protein Interaction Mapping - methods
Protein-protein interactions
Proteins
Proteins - chemistry
Proteins - metabolism
Structural biology
Technology
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Summary:A comprehensive understanding of protein-protein interactions is an important next step in our quest to understand how the information contained in a genome is put into action. Although a number of experimental techniques can report on the existence of a protein- protein interaction, very few can provide detailed structural information. NMR spectroscopy is one of these, and in recent years several complementary NMR approaches, including residual dipolar couplings and the use of paramagnetic effects, have been developed that can provide insight into the structure of protein-protein complexes. In this article, we review these approaches and comment on their strengths and weaknesses.
ISSN:1615-9853
1615-9861
1615-9861
DOI:10.1002/pmic.200900303