The McKnight lab is interested in the folding, function and dynamics of proteins. A long-time favorite model system is the actin-binding \u201cheadpiece\u201d 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.<\/p>\n
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\nFacility for Structural NMR<\/a><\/p>\n","protected":false},"author":1811,"template":"","_links":{"self":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/profile\/20954"}],"collection":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/profile"}],"about":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/types\/profile"}],"author":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/users\/1811"}],"version-history":[{"count":8,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/profile\/20954\/revisions"}],"predecessor-version":[{"id":23930,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/profile\/20954\/revisions\/23930"}],"wp:attachment":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/media?parent=20954"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}