Vicinal Disulfide Bridge Conformers by Experimental Methods and by Ab Initio and DFT Molecular Computations

Ilona Hudáky, Zoltán Gáspári, Oliviero Carugo, Maša Čemažar, Sándor Pongor, András Perczel

Research output: Article

26 Citations (Scopus)


A systematic comparison is made between experimental and computational data gained on vicinal disulfide bridges in proteins and peptides. Structural and stability data of ab initio and density functional theory (DFT) calculations on the model compound 4,5-ditiaheptano-7-lactam and the model peptide HCO-ox-[Cys-Cys]-NH2 at RHF/3-21G*, B3LYP/6-31+G(d), and B3LYP/6-311++G(d,p) levels of theory are presented. The data on Xxx-Cys-Cys-Yyy type amino acid sequence units retrieved from PDB SELECT, along with data on sequence units that have vicinal disulfide bridge, taken from the Brookhaven Protein Data Bank, are conformationally characterized. Amino acid backbone conformations, cis-trans isomerism of the amide bond between the two cysteine residues, and ring puckering are studied. Ring puckers are characterized by their relation to the conformers of the parent 4,5-ditiaheptano-7-lactam. Computational precision and accuracy are proved by frequency calculation and solvent model optimization on selected conformers. It is found that the ox-[Cys-Cys] unit is able to accept types I, II, VIa, VIb, and VIII β-turn structures.

Original languageEnglish
Pages (from-to)152-168
Number of pages17
JournalProteins: Structure, Function and Genetics
Issue number1
Publication statusPublished - ápr. 1 2004

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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