title: Peptide alpha-helicity in aqueous trifluoroethanol: correlations with predicted alpha-helicity and the secondary structure of the corresponding regions of bovine growth hormone.
abstract: The relationship between trifluoroethanol (TFE) enhancement of peptide alpha-helicity and protein secondary structure has been studied for a series of 11 peptides which span the complete primary sequence of bovine growth hormone (bGH). Ten of these peptides become increasingly alpha-helical as the solution concentration of TFE is increased. The amount of alpha-helicity developed by these peptides plateaus above 10 mol % TFE and ranges from 0 to 71%. The increased alpha-helicity, as determined by CD, closely correlates with the amount of alpha-helix predicted for eight of the eleven peptides analyzed (r = 0.9). Therefore, for this group of peptides, it appears that this technique can be used as a measure of alpha-helical propensity. Inclusion of the remaining three peptides in this analysis significantly lowers the correlation (r = 0.6). The reduced correspondence between TFE-enhanced and predicted alpha-helicity in this latter subset of peptides may be due to their relatively high hydrophobicity. In addition, the relevance of TFE-enhanced peptide alpha-helicity and the secondary structure of the corresponding protein regions was explored. Although the three peptides which form the largest amount of alpha-helicity in the presence of 10 mol % TFE correspond to alpha-helical regions of the protein, the overall correlation is significantly lower than is observed for the TFE-enhanced and predicted alpha-helicity. These findings suggest that the propensity of specific amino acid sequences for alpha-helix formation influences the amount of alpha-helicity which forms in corresponding protein sequences, but that other factors can modify this structure.
authors.affiliation: Control Biotechnology, Upjohn Company, Kalamazoo, Michigan 49001.
authors.forename: S R
authors.initials: SR
authors.lastname: Lehrman
authors.forename: J L
authors.initials: JL
authors.lastname: Tuls
authors.forename: M
authors.initials: M
authors.lastname: Lund
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D013006:Growth Hormone; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D014270:Trifluoroethanol; D014867:Water
chemical_list: D010446:Peptide Fragments; D014867:Water; D014270:Trifluoroethanol; D013006:Growth Hormone