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oai:www.ideals.illinois.edu:2142/85441 2023-07-11 col_2142_5131 col_2142_14828 com_2142_5130 com_2142_14827 com_2142_14793 com_2142_8903

Martin Gruebele Nguyen, Houbi Tung Thanh 2015-09-25T22:46:06Z 2015-09-25T22:46:06Z 10000-01-01 2004 2004 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. To complete our work we summarize ongoing research on the membrane interactions of a small alpha-helical peptide. Made available in DSpace on 2015-09-25T22:46:06Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3160934.pdf: 17970937 bytes, checksum: 6aaa6c50cfe3ab7c6adf68a9c7951f92 (MD5) Previous issue date: 2004 Embargo set by: Seth Robbins for item 86722 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 320 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2004. http://hdl.handle.net/2142/85441 (MiAaPQ)AAI3160934 eng Biophysics, General A Survey of Beta-Sheet Folding: WW Domains With Zinc Fingers and Membrane Peptides text Biophysics and Computational Biology Biophysics and Computational Biology University of Illinois at Urbana-Champaign Dissertation Ph.D.