C. James McKnight, Ph.D.
Associate Provost and Dean of Graduate Medical Sciences Associate Professor of Pharmacology, Physiology & Biophysics
The McKnight lab is interested in the folding, function and dynamics of proteins. A long-time favorite model system is the actin-binding “headpiece” domain of the protein villin. The villin headpiece contains a subdomain of only 35-residues that folds to form a novel three helix structure (HP35). HP35 is one of the shortest amino acid sequences that folds to a monomeric native state in the absence of disulfide bonds or bound metals/ligands. We use NMR, circular dichroism spectroscopy, and other methods, to investigate the stability and motions of proteins using the unique HP35 domain as well as other small protein domains.
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Facility for Structural NMR