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Updated: Aug 25, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
Engineering and design of ligand-induced conformational change in proteins
Laura S Mizoue1, Walter J Chazin
1Department 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.
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