Gierasch Lab








Principal Research Interests

Protein Folding
    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 of the in vitro folding of a predominantly β–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 also 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?

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