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Protein Fold Evolution

Structures of p22 arc wildtype and switch mutant

This project explored how protein structures evolve from one fold to another. By swapping two consecutive residues in the dimeric DNA-binding protein arc-repressor of phage p22, we converted an intermonomer beta strand to two interacting helices. The demonstration that simple mutations can interconvert protein secondary structures has important implications for how proteins evolve into new folds, in vivo. This project was a collaboration with Drs. Matthew Cordes, now at the University of Arizona, and Robert Sauer at MIT.



Last Revised 04/14/05

©2000 Jamie McKnight