A single-residue affinity scale for DNA-binding using linear perceptron
Andrabi, Munazah
Ahmad, Shandar
10.4225/03/5a137307c9ae7
https://bridges.monash.edu/articles/dataset/A_single-residue_affinity_scale_for_DNA-binding_using_linear_perceptron/5619538
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) ;
Coverage:
Rights: Copyright by Third IAPR International Conference on Pattern Recognition in Bioinformatics. All rights reserved.
2017-11-21 00:27:50
Bioinformatics -- Congresses
Computational biology -- Congresses
Computer vision in medicine -- Congresses
Computational biology -- Methods -- Congresses
Pattern recognition, automated -- Methods -- Congresses
DNA-binding
Perceptron
Free energy
2008
conference paper
1959.1/63731
monash:7872
Bioinformatics Software
Bioinformatics
Pattern Recognition and Data Mining