DocumentCode
2766961
Title
Domain-domain interactions in obligate and non-obligate protein-protein interactions
Author
Maleki, Mina ; Rueda, Luis
Author_Institution
Sch. of Comput. Sci., Univ. of Windsor, Windsor, ON, Canada
fYear
2011
fDate
12-15 Nov. 2011
Firstpage
907
Lastpage
908
Abstract
In this study, an analysis of protein-protein interactions (PPIs) that uses properties of domain-domain interactions (DDIs) present in the interface is discussed. The aim is to predict obligate and non-obligate complexes. The results show that support vector machines (SVM) classifier achieves much better prediction performance, even better than linear dimensionality reduction (LDR) schemes and aslo desolvation energy is better than interface area and composition for predicting transient and obligate complexes. Moreover, a visual and numerical analysis insight of the distribution of the DDIs in different complexes is shown that most homo-domain pairs are in obligate interactions.
Keywords
biology computing; molecular biophysics; numerical analysis; proteins; support vector machines; desolvation energy; domain-domain interactions; homo-domain pairs; linear dimensionality reduction; numerical analysis; protein-protein interactions; support vector machine classifier; Accuracy; Amino acids; Bioinformatics; Protein engineering; Proteins; Support vector machines; Transient analysis; complex type prediction; domain-domain interaction; protein-protein interaction;
fLanguage
English
Publisher
ieee
Conference_Titel
Bioinformatics and Biomedicine Workshops (BIBMW), 2011 IEEE International Conference on
Conference_Location
Atlanta, GA
Print_ISBN
978-1-4577-1612-6
Type
conf
DOI
10.1109/BIBMW.2011.6112498
Filename
6112498
Link To Document