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Analysis of Protein Protein Dimeric Interfaces
Bioinformatics and Computational Biology Proceedings and Presentations
  • Feihong Wu, Iowa State University
  • Fadi Towfic, Iowa State University
  • Drena Dobbs, Iowa State University
  • Vasant Honavar, Iowa State University
Document Type
Conference Proceeding
Publication Version
Accepted Manuscript
Publication Date
Conference Title
2007 IEEE International Conference on Bioinformatics and Biomedicine
Conference Date
November 2-4, 2007
(37.5482697, -121.98857190000001)

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.


This is a proceeding from IEEE International Conference on Bioinformatics and Biomedicine (2007): 35, doi: 10.1109/BIBM.2007.60. Posted with permission.

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Citation Information
Feihong Wu, Fadi Towfic, Drena Dobbs and Vasant Honavar. "Analysis of Protein Protein Dimeric Interfaces" Fremont, California(2007) p. 35 - 41
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