Solution conformation of N-terminal fragments of trichosanthin small domain (TCS 182-200). Circular dichroic studies. NLM AIDSLINE Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

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Solution conformation of N-terminal fragments of trichosanthin small domain (TCS 182-200). Circular dichroic studies.

J Pept Res. 1997 Feb;49(2):113-9. Unique Identifier : AIDSLINE MED/97292797
Hu HY; Lu ZX; Du YC; Shanghai 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.
Keywords: *Trichosanthin/CHEMISTRYKWDtrichosanthin/chemistry
970930
M9791365

Copyright © 1997 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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