Juxtaposed Half-Cystines as Disulphide Bridged Partners in Protein Tertiary Structure

Kunchur      Guruprasad; V.   J.   Kartik; T.      Lavanya; Lalitha      Guruprasad

doi:10.2174/092986606777145841

Abstract

Disulphide bridges involving juxtaposed half-cystines are observed in a number of protein three-dimensional structures analyzed from the Protein Data Bank. These disulphide bridges comprise a ring of 8-atoms corresponding to Cα1-C-N-Cα2-Cβ2-Sγ2-Sγ1-Cβ1-Cα1 in the two half-cystines. The presence of such disulphide bridges introduces a bend or kink in the protein polypeptide chain.

Keywords: Protein Data Bank (PDB), Disulphide Bridges, neurotoxin, Cys83, oxidoreductases

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Protein & Peptide Letters

Title: Juxtaposed Half-Cystines as Disulphide Bridged Partners in Protein Tertiary Structure

Volume: 13 Issue: 6

Author(s): Kunchur Guruprasad, V. J. Kartik, T. Lavanya and Lalitha Guruprasad

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Keywords: Protein Data Bank (PDB), Disulphide Bridges, neurotoxin, Cys83, oxidoreductases

Abstract: Disulphide bridges involving juxtaposed half-cystines are observed in a number of protein three-dimensional structures analyzed from the Protein Data Bank. These disulphide bridges comprise a ring of 8-atoms corresponding to Cα1-C-N-Cα2-Cβ2-Sγ2-Sγ1-Cβ1-Cα1 in the two half-cystines. The presence of such disulphide bridges introduces a bend or kink in the protein polypeptide chain.

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Guruprasad Kunchur, Kartik J. V., Lavanya T. and Guruprasad Lalitha, Juxtaposed Half-Cystines as Disulphide Bridged Partners in Protein Tertiary Structure, Protein & Peptide Letters 2006; 13 (6) . https://dx.doi.org/10.2174/092986606777145841