Lila M. Gierasch
Distinguished Professor, Department of Biochemistry and Molecular Biology and Department of Chemistry, University of Massachusetts
Editor-in-Chief, The Journal of Biological Chemistry; Ralph F. Hirschmann Award in Peptide Chemistry, American Chemical Society
Ph.D.: Harvard University Honors: A.P. Sloan Fellowship; Vincent du Vigneaud Award for Young Investigators in Peptide Chemistry; Guggenheim Fellowship; Fellow, American Association for the Advancement of Science; NIH Pioneer Award; Dorothy Hodgkin Award of the Protein Society
The protein folding problem, namely how amino acid sequence determines the three-dimensional structure of a protein, is not fully understood despite many years of effort. We are addressing this problem in a variety of ways in our laboratory: We study the conformational preferences of model peptides in order to explore how local sequence guides folding. We are also carrying out detailed studies in the in vitro folding of a predominantly b -sheet protein with a very simple topology. Methods we use in all of our folding work include circular dichroism, fluorescence, and nuclear magnetic resonance. We are particularly interested in how a protein folds in vivo. In recent years, a class of proteins called molecular chaperones has been found to facilitate protein folding in vivo. We are addressing several questions concerning chaperones: How do they recognize and bind incompletely folded polypeptides? Do different classes of chaperones bind to their substrates in distinct ways? How do chaperones interact with their co-chaperones? Is the mechanism of chaperone-mediated folding different from that of the isolated protein?