Protein-protein interaction analysis by nuclear magnetic resonance spectroscopy
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Authors
Thompson, Peter M.
Beck, Moriah R.
Campbell, Sharon L.
Advisors
Issue Date
2015
Type
Book chapter
Keywords
Nuclear magnetic resonance (NMR) , Protein-protein interaction , Chemical-shift perturbation (CSP) , Paramagnetic relaxation enhancement (PRE) , Docking
Citation
Thompson, Peter M.; Beck, Moriah R.; Campbell, Sharon L. 2015. Chapter 16 -- Protein-protein interaction analysis by nuclear magnetic resonance spectroscopy, In: Protein-Protein Interactions, vol. 1278 of the series Methods in Molecular Biology, pp 267-279
Abstract
Nuclear magnetic resonance (NMR) has continued to evolve as a powerful method, with an increase in the number of pulse sequences and techniques available to study protein-protein interactions. In this chapter, a straightforward method to map a protein protein interface and design a structural model is described, using chemical shift perturbation, paramagnetic relaxation enhancement, and data-driven docking.
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Publisher
Springer New York
Journal
Book Title
Series
PubMed ID
DOI
ISSN
1064-3745