NMR insights into protein allostery

Gregory Manley; J Patrick Loria

doi:10.1016/j.abb.2011.10.023

NMR insights into protein allostery

Arch Biochem Biophys. 2012 Mar 15;519(2):223-31. doi: 10.1016/j.abb.2011.10.023. Epub 2011 Dec 16.

Authors

Gregory Manley¹, J Patrick Loria

Affiliation

¹ Department of Chemistry, Yale University, 225 Prospect Street, P.O. Box 208107, New Haven, CT 06520-8107, USA.

Abstract

Allosterism is one of nature's principal methods for regulating protein function. Allosterism utilizes ligand binding at one site to regulate the function of the protein by modulating the structure and dynamics of a distant binding site. In this review, we first survey solution NMR techniques and how they may be applied to the study of allostery. Subsequently, we describe several examples of application of NMR to protein allostery and highlight the unique insight provided by this experimental technique.

Publication types

Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review

MeSH terms

Allosteric Regulation
Kinetics
Movement
Nuclear Magnetic Resonance, Biomolecular / methods*
Proteins / chemistry*
Proteins / metabolism*

Substances

Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding