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 :
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