학술논문
Theoretical study of a nonpeptidic polydisulfide α-helix.
Document Type
Article
Source
Subject
*PEPTIDES
*DISULFIDES
*CARBON
*SULFUR
*MOLECULES
*DENSITY functionals
*NUMERICAL calculations
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Language
ISSN
1741-5993
Abstract
A carbon–sulfur molecule has been designed as a mimic of peptides. Density functional theory calculations showed that the oxidation of 10 moles of methanedithiol led to a polydisulfide oligomer, HS (CH2SS)9CH2SH. The polydisulfide can adopt an α -helix type of secondary structure, where the chain is coiled. Unlike proteins, the S–S bonds in the polydisulfide function as secondary rather than tertiary structural elements. The helix contains 8 non-hydrogen atoms per turn, 2.7 Å methylenes per turn, a pitch distance of 8.6 Å, and a radius of 1.00 Å. The methylene sites could carry R group residues similar to amino acids. [ABSTRACT FROM PUBLISHER]