Format

Send to

Choose Destination
Curr Opin Struct Biol. 2002 Aug;12(4):459-63.

Engineering and design of ligand-induced conformational change in proteins.

Author information

1
Department of Biochemistry, Center for Structural Biology, 896 PRB, Vanderbilt University, Nashville, TN 37232-0146, USA. l.mizoue@vanderbilt.edu

Abstract

The ability to manipulate ligand-induced conformational change, although representing a major challenge to the protein engineer, is an essential end point in efforts to produce novel functional proteins for biotechnology and therapeutic applications. Progress towards this goal requires determining not only what factors control the fold and stability of a protein, but also how ligand binding alters the complex conformational/energetic landscape. Important strides are being made on several fronts, including understanding the origin of long-range effects and allosteric structural mechanisms, using both experimental and theoretical approaches.

PMID:
12163068
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center