
SEMINAR
March 28 (Fri) 2008, 11AM- SE
213
Predicting protein-protein interactions in highly
mutating sequence positions of RNA retroviruses genomes using Mutual
Information
Scooter
Willis, Department of Computer and Information
Science and Engineering,
Abstract
All biological functions in the
living cell involve the interaction of protein structures in a complex system
where through billions of years of evolution the insertion, deletion and
mutation of DNA sequences provides the coding for life as we know it. The
challenge in understanding this coding is the ability to separate random
mutations from positive mutations that are critical to preserving or improving
the functional/structural properties of the protein interactions. Mutual
Information is used to calculate the mutual dependence between two sequence
positions which indicates the information that may describe the importance of
compensating mutations.
The application of Mutual
Information between two variables is straightforward given that the calculated
probability distributions are accurate. Numerous papers have been published on
the use of Mutual Information against sequence data to detect compensating
mutations with techniques to filter false positives or compensate for the phylogenetic effect associated with using closely related
sequence data. The Reduced Phylogenetic Effect (RPE)
method is introduced to measure the mutation distributions based on mutations
events in the phylogenetic tree resulting in an
improved detection of coevolving sequence positions.
The RPE method is used to predict
protein-protein interactions as a network topology for HIV, HCV, Influenza A,
and Dengue fever which are retroviruses that have high mutation rates, small
genomes and (because of the impact of these diseases) are aggressively
researched. Current wet lab research techniques used to detect or validate
protein interactions in viruses is an evolving field. The use of readily available
virus sequence data from wet lab experiments and the RPE method to detect
protein interactions can provide invaluable insight into the protein topology
or systems biology of a virus.
Contact for more details: rnarayan@fau.edu,
URL: http://www.science.fau.edu/fbrcf/