Towards a Hybrid Method for Detecting Critical Protein Residues
Document Type
Conference Proceeding
Department or Administrative Unit
Computer Science
Publication Date
10-4-2012
Abstract
Some regions in proteins play a critical role in determining their structure and function. Examples include flexible regions such as hinges which allow domain motions, and highly conserved functional interfaces which allow interactions with other proteins. Detecting these regions facilitates the analysis and simulation of protein rigidity and conformational changes and aids in characterizing protein-protein binding. We present an analysis of critical residues in proteins using a combination of two complementary methods. One method performs rigidity analysis to find rigid clusters of amino acids in a protein and the other method uses evolutionary conservation to find functional interfaces in proteins. We applied both methods to a dataset of proteins, including proteins with experimentally known critical residues. The results show that the combination of the two methods can detect the vast majority of critical residues in tested proteins.
Recommended Citation
Akbal-Delibas, B., Jagodzinski, F., & Haspel, N. (2012). Towards a hybrid method for detecting critical protein residues. 2012 IEEE International Conference on Bioinformatics and Biomedicine Workshops. https://doi.org/10.1109/bibmw.2012.6470240
Journal
2012 IEEE International Conference on Bioinformatics and Biomedicine Workshops
Rights
Copyright © 2012, IEEE
Comments
This article was originally published in 2012 IEEE International Conference on Bioinformatics and Biomedicine Workshops. The full-text article from the publisher can be found here.
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