Solution conformation of N-terminal fragments of trichosanthin small domain (TCS 182-200). Circular dichroic studies.
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.
Hu
H Y
HY
Shanghai Institute of Biochemistry, Chinese Academy of Sciences, People's Republic of China.
Lu
Z X
ZX
Du
Y C
YC
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015978:Trichosanthin / Q000737:chemistry*
D015978:Trichosanthin