Protein-Inhibitor Interaction Studies Using NMR

Solution-state NMR has been widely applied to determine the threedimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment,...

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Bibliographic Details
Published inApplications of NMR Spectroscopy Vol. 1; no. 1; pp. 143 - 181
Main Author Ishima, Rieko
Format Book Chapter Journal Article
LanguageEnglish
Published United Arab Emirates 01.01.2015
Subjects
Drug
NMR
inhibitor
protein
relaxation
interaction
structure
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Summary:Solution-state NMR has been widely applied to determine the threedimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment, such as molecular mass and knowledge of the primary structure, is unique for proteins compared to small molecules. In this review article, protein NMR for structural biology is introduced with comparisons to small-molecule NMR, such as descriptions of labeling strategies and the effects of molecular dynamics on relaxation. Next, applications for protein NMR are reviewed, especially practical aspects for protein-observed ligand-protein interaction studies. Overall, the following topics are described: (1) characteristics of protein NMR, (2) methods to detect protein-ligand interactions by NMR, and (3) practical aspects of carrying out protein-observed inhibitor-protein interaction studies.
ISSN:2405-4674
DOI:10.2174/9781608059621115010007