Analysis of protein protein dimeric interfaces

Feihong Wu, Fadi Towfic, Drena Dobbs, Vasant Honavar

Research output: Chapter in Book/Report/Conference proceedingConference contribution

7 Scopus citations

Abstract

We analyzed the structural properties and the local surface environment of surface amino acid residues of proteins using a large, non-redundant dataset of 2383 protein chains in dimeric complexes from PDB. We compared the interface residues and non-interface residues based on six properties: side chain orientation, surface roughness, solid angle, cx value, hydrophobicity and interface cluster size. The results of our analysis show that interface residues have side chains pointing inward; interfaces are rougher, tend to be flat, moderately convex or concave and protrude more relative to non-interface surface residues. Interface residues tend to be surrounded by hydrophobic neighbors and tend to form clusters consisting of three or more interfaces residues. These findings are consistent with previous published studies using much smaller datasets, while allowing for more qualitative conclusions due to our larger dataset. Preliminary results suggest the possibility of using the six the properties to identify putative interface residues.

Original languageEnglish (US)
Title of host publicationProceedings - 2007 IEEE International Conference on Bioinformatics and Biomedicine, BIBM 2007
Pages35-41
Number of pages7
DOIs
StatePublished - 2007
Event2007 IEEE International Conference on Bioinformatics and Biomedicine, BIBM 2007 - Fremont, CA, United States
Duration: Nov 2 2007Nov 4 2007

Publication series

NameProceedings - 2007 IEEE International Conference on Bioinformatics and Biomedicine, BIBM 2007

Other

Other2007 IEEE International Conference on Bioinformatics and Biomedicine, BIBM 2007
CountryUnited States
CityFremont, CA
Period11/2/0711/4/07

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Computer Science(all)
  • Biomedical Engineering

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