A single-residue affinity scale for DNA-binding using linear perceptron
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A linear scale to estimate DNA-binding free energy of amino acid residues is reported. Scales derived exclusively for irregular and helical positions give 76% and 68% classification accuracy between stabilizing and destabilizing protein-DNA interaction. Mean absolute error (MAE) in ddG values is 0.786 and 0.883 kcal/mol respectively. Without using structure information of residues to derive affinity scales, 67.0% mutations could be correctly classified between those stabilizing and destabilizing binding. Mean absolute error (MAE) and correlation of ddG predictions are 0.953 kcal/mol and 0.385 respectively. PRIB 2008 proceedings found at: http://dx.doi.org/10.1007/978-3-540-88436-1
Contributors: Monash University. Faculty of Information Technology. Gippsland School of Information Technology ;
Chetty, Madhu ;
Ahmad, Shandar ;
Ngom, Alioune ;
Teng, Shyh Wei ;
Third IAPR International Conference on Pattern Recognition in Bioinformatics (PRIB) (3rd : 2008 : Melbourne, Australia) ;
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Rights: Copyright by Third IAPR International Conference on Pattern Recognition in Bioinformatics. All rights reserved.
提供机构：
Monash University
创建时间：
2026-02-11
