{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85441"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85441","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"A Survey of Beta-Sheet Folding: WW Domains With Zinc Fingers and Membrane Peptides","abstract":"This work describes the present state of folding research involving small, fast-folding protein systems. By perturbing a WW domain sequence with side-chain mutations, truncations, amide-to-ester exchanges, and loop rearrangements we find that loop structures can dictate the folding dynamics of this model beta-sheet protein. We then report on a synthetic zinc-finger peptide used to bridge the gap between experimental and theoretical protein folding research. 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