I am currently at the University of Illinois, Urbana-Champaign. I will arrive at Brandeis in the summer of 2001.
Proteins are dynamic molecules whose motions are important for folding, function and stability.
Our laboratory uses optical techniques, particularly fluorescence, to study protein conformation and folding in real time. We are interested in elucidating the relationships between protein dynamics and other protein properties such as protein function and stability. For fluorescence studies, observed fluorophores may be native to the protein, such as the amino acids tyrosine and tryptophan, or extrinsic covalently attached labels. Bulk fluorescence studies measure the average values for a population while single molecule techniques allow measurements to be performed on individual fluorescently labeled proteins. Single molecule experiments can reveal details about a population such as conformational substates and whether all members behave identically.