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- W316804580 abstract "Publisher Summary This chapter elaborates the conformational analysis of bovine growth hormone (bGH) fragments which correspond to helical regions of the intact protein. Porcine growth hormone has been shown to be an antiparallel four helix bundle protein. The strong homology between porcine and bovine growth hormones suggests that the two proteins have similar tertiary structure. The determination of the secondary structure of bovine growth hormone fragments which form α-helices within the intact protein is described. It is demonstrated that synthetic and proteolytic fragments or bGH, which include residues 109 to 133, form α-helices in aqueous solution. The synthesis and conformational analysis of peptide fragments which correspond to helices 2 and 4 of the putative four helix bundle, and fragments which correspond to nonhelical regions of bGH is reported. It is found that [164-Ser-153-180]-bGH has a greater propensity for a-helix formation in aqueous alcohol than [78-97]-bGH, or peptides which are derived from nonhelical regions of the protein. The conformational properties of these bGH fragments have been studied as a function of temperature, and trifluoroethanol, peptide and denaturant concentration." @default.
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- W316804580 date "1989-01-01" @default.
- W316804580 modified "2023-09-27" @default.
- W316804580 title "CONFORMATIONAL ANALYSIS OF BOVINE GROWTH HORMONE FRAGMENTS WHICH CORRESPOND TO HELICAL REGIONS OF THE INTACT PROTEIN" @default.
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- W316804580 doi "https://doi.org/10.1016/b978-0-407-01473-2.50026-6" @default.
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