| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1925614 | Archives of Biochemistry and Biophysics | 2012 | 9 Pages |
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.
► Solution NMR provides unique structural and dynamical detail of allosteric proteins. ► Relaxation dispersion experiments provide evidence for lowly populated conformers. ► NMR can provide insight into kinetics and thermodynamics of allostery.
