Affiliations: Supercomputer Education and Research Centre,
Bangalore, India | Bioinformatics Centre, Indian Institute of Science,
Bangalore, India
Note: [] Corresponding author: Debnath Pal, Bioinformatics Centre, Indian
Institute of Science, Bangalore-560012, India. Tel.: +91 80 2293 2901; Fax: +91
80 2360 0551; E-mail: [email protected]
Abstract: Apoptosis is a programmed mechanism of cell death that is a normal
component of development and health of multi-cellular organisms. In this study,
we ask if interface properties of apoptotic protein complexes are
different from protein complexes in general. We find that although in
apoptotic protein complexes the overall distribution of interface size,
surface complementarity, hydrogen bonding, hydrophobicity are similar to
general interface properties, apoptotic complexes tend to have more
fragmented interfaces and different secondary structural preferences. The
statistics on the number of interfaces where specific amino acid(s) occur with
significantly enhanced frequency suggest that Arg, Met and Asp are most
important functional residues. The role of Met is believed to be unique, as
evidenced from the existing data on hot spot potential of residues. These
findings together provide insight into the possible role of various
physico-chemical attributes at the protein interface in regulation of the apoptosis process.
Keywords: Apoptosis, protein-protein interaction, residue propensity, protein interface, secondary structure
