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Default The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation

The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation

Available online 13 December 2012
Publication year: 2012
Source:Current Opinion in Structural Biology



Historically it has been virtually impossible to experimentally determine the contribution of residual protein entropy to fundamental protein activities such as the binding of ligands. Recent progress has illuminated the possibility of employing NMR relaxation methods to quantitatively determine the role of changes in conformational entropy in molecular recognition by proteins. The method rests on using fast internal protein dynamics as a proxy. Initial results reveal a large and variable role for conformational entropy in the binding of ligands by proteins. Such a role for conformational entropy in molecular recognition has significant implications for enzymology, signal transduction, allosteric regulation and the development of protein-directed pharmaceuticals.
Graphical abstract

Highlights

? Fast motion interconverts states with significant conformational entropy. ? Fast internal motion can be characterized in a site resolved way using solution NMR relaxation phenomena. ? Internal protein motion can be used as a proxy for conformational entropy. ? Conformational entropy can contribute significantly to ligand binding by proteins.





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