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Construction and Systematical Symmetric Studies of a Series of Supramolecular Clusters with Binary or Ternary Ammonium Triphenylacetates
Published on: February 15, 2016
Solution conformation of N-terminal fragments of trichosanthin small domain (TCS 182-200). Circular dichroic studies
1Shanghai Institute of Biochemistry, Chinese Academy of Sciences, People's Republic of China.
Abstract:
Three peptides, T14, T18 and TDK, derived from the N-terminus of trichosanthin small domain (TCS 182-200) have been investigated by circular dichroism. Secondary structure and structural transitions of the above peptides under different conditions were studied. Alcohol prompts a transition of the T18 peptide from a beta-sheet to an alpha-helical structure. It also increases the alpha-helicities of T14 and TDK. The beta-sheet of T18 peptide appears more hydrophobic than the alpha-helix of T14 or TDK. The effects of polypeptide sequence and solvent on secondary structure formation of these model peptides are discussed.

