Related Experiment Video
Updated: May 25, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Predicting functional residues of protein sequence alignments as a feature selection task
Chris Haddow1, Justin Perry, Marcus Durrant
1School of Computing, Engineering, and Information Sciences, Northumbria University, Newcastle NE2 1XE, UK. chris.haddow@northumbria.ac.uk
Abstract:
Determining which residues within a multiple alignment of protein sequences are most responsible for protein function is a difficult and important task in bioinformatics. Here, we show that this task is an application of the standard Feature Selection (FS) problem. We show the comparison of standard FS techniques with more specialised algorithms on a range of data sets backed by experimental evidence, and find that some standard algorithms perform as well as specialised ones. We also discuss how considering the discriminating power of combinations of residue positions, rather than the power of each position individually, has the potential to improve the performance of such algorithms.
More Related Videos
Related Concept Videos
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Protein Families
Protein-protein Interfaces
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Predicting Products: Substitution vs. Elimination
The following factors can influence the mechanisms competing against each other:
Signal Sequences and Sorting Receptors

