title: Environment affects amino acid preference for secondary structure.
abstract: Three equivocal amino acid sequences were synthesized that are predicted to be alpha-helical from amino acid preference but are found to be primarily beta-strand from x-ray diffraction of their respective proteins. In some solvent systems we recover the alpha-helical structure predicted by amino acid preference, whereas in other systems we mimic the interior of the protein and produce a beta-strand. These results are experimental proof that the environment is important in determining the secondary structure formed by an amino acid sequence; therefore schemes that predict secondary structure from amino acid sequence alone can never be totally successful.
authors.affiliation: Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331-6503.
authors.forename: L
authors.initials: L
authors.lastname: Zhong
authors.forename: W C
authors.initials: WC
authors.lastname: Johnson
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides