Zavodszky lab
Flexibility at protein-protein interfaces
The ability to reconstruct and study biological pathways greatly depends on how well we can predict the mode of interaction between the elements of the pathways, which are usually proteins of various functions. Given the structures of the free proteins, current computational docking tools cannot predict the structure of the bound complex when one or both or the binding partners undergo large conformational changes. Based on flexibility analysis of the unbound structure using the graph-theoretical algorithm FIRST, it is possible to predict what parts of the protein are most likely to undergo conformational changes. Large-scale movements of the predicted flexible parts can be modeled using clever algorithms that sample only the low frequency modes of the possible motions.
Department of Biochemistry and Molecular Biology
Michigan State University
Biomedical and Physical Sciences Building Room 4216
East Lansing, MI, 48824-1319
Phone: (517) 432-7177 Fax: (517) 353 9334
Email: zavodszk@msu.edu
Back to the lab web page