• Francis Rodier

      Articles written in Journal of Biosciences

    • Peptide segments in protein-protein interfaces

      Arumay Pal Pinak Chakrabarti Ranjit Bahadur Francis Rodier Joël Janin

      More Details Abstract Fulltext PDF

      An important component of functional genomics involves the understanding of protein association. The interfaces resulting from protein-protein interactions –

      specific, as represented by the homodimeric quaternary structures and the complexes formed by two independently occurring protein components, and

      non-specific, as observed in the crystal lattice of monomeric proteins – have been analysed on the basis of the length and the number of peptide segments.

      In 1000 Å2 of the interface area, contributed by a polypeptide chain, there would be 3.4 segments in homodimers, 5.6 in complexes and 6.3 in crystal contacts. Concomitantly, the segments are the longest (with 8.7 interface residues) in homodimers. Core segments (likely to contribute more towards binding) are more in number in homodimers (1.7) than in crystal contacts (0.5), and this number can be used as one of the parameters to distinguish between the two types of interfaces. Dominant segments involved in specific interactions, along with their secondary structural features, are enumerated.

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