z-logo
open-access-imgOpen Access
Protein residues determining interaction specificity in paralogous families
Author(s) -
Borja Pitarch,
Juan A. G. Ranea,
Florencio Pazos
Publication year - 2020
Publication title -
bioinformatics
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btaa934
Subject(s) - interactome , pairwise comparison , sequence (biology) , computational biology , computer science , set (abstract data type) , multiple sequence alignment , biology , sequence alignment , data mining , theoretical computer science , peptide sequence , genetics , artificial intelligence , gene , programming language
Predicting the residues controlling a protein's interaction specificity is important not only to better understand its interactions but also to design mutations aimed at fine-tuning or swapping them as well.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom