Journal
BIOINFORMATION
Volume 1, Issue 4, Pages 121-+Publisher
BIOMEDICAL INFORMATICS
DOI: 10.6026/97320630001121
Keywords
protein-protein interaction; interface analysis; hot spot residues; inter-atomic interaction
Categories
Funding
- NANYANG Technological University, Singapore
Ask authors/readers for more resources
It is known that binding free energy of protein-protein interaction is mainly contributed by hot spot (high energy) interface residues. Here, we investigate the characteristics of hot spots by examining inter-atomic sidechain-sidechain interactions using a dataset of 296 alanine-mutated interface residues. Results show that hot spots participate in strong and energetically favorable sidechain-sidechain interactions. Subsequently, we describe a novel, yet simple 'hot spot' prediction model with an accuracy that is similar to many available approaches. The model is also shown to efficiently distinguish specific protein-protein interactions from non-specific interactions.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available