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

abstract

• 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.

authors

• Wand, Joshua

published proceedings

• Curr Opin Struct Biol

author list (cited authors)

• Wand, A. J.

citation count

• 138

complete list of authors

• Wand, A Joshua

publication date

• February 2013

publisher

• Elsevier  Publisher

published in

• Current Opinion in Structural Biology  Journal

keywords

• Entropy
• Ligands
• Nuclear Magnetic Resonance, Biomolecular
• Protein Binding
• Protein Conformation
• Proteins

PubMed Central ID

• 23246280

Digital Object Identifier (DOI)

• 10.1016/j.sbi.2012.11.005

start page

• 75

end page

• 81

volume

• 23

issue

• 1

URL

• http://dx.doi.org/10.1016/j.sbi.2012.11.005