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Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy
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Date
2009-06-15
Author
Tunçbağ, Nurcan
Keskin, Ozlem
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Motivation: Hot spots are residues comprising only a small fraction of interfaces yet accounting for the majority of the binding energy. These residues are critical in understanding the principles of protein interactions. Experimental studies like alanine scanning mutagenesis require significant effort; therefore, there is a need for computational methods to predict hot spots in protein interfaces.
Subject Keywords
Globular-Proteins
,
Subunit İnterfaces
,
Receptor Complex
,
Binding-Energy
,
Sequence
,
Prediction
,
Conservation
,
Database
,
Hormone
URI
https://hdl.handle.net/11511/32060
Journal
BIOINFORMATICS
DOI
https://doi.org/10.1093/bioinformatics/btp240
Collections
Graduate School of Informatics, Article
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N. Tunçbağ and O. Keskin, “Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy,”
BIOINFORMATICS
, pp. 1513–1520, 2009, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/32060.