Investigating protein features contribute to salt stability of halolysin proteins

Journal of Cell and Molecular Research

Article 2, Volume 2, Issue 1 - Serial Number 3, January 0, Pages 15-28   

DOI: 10.22067/jcmr.v2i1.3144

Authors

Mansour Ebrahimi^* ; Esmaeil Ebrahimie; Narjes Rahpayma

Shiraz University

Abstract

We used various screening techniques, clustering, decision tree and generalized rule induction (association) (GRI) models and molecular phylogenic relationship to search for patterns of halophi-licy and to find features contribute to halolysin salt stability. We found Met was the sole N-terminal amino acid in halolysin proteins, whereas other amino acids found at this position of oth-er proteases and termitase. Eighty-three protein features were shown to be important in feature selection modeling, and just one peer group with an anomaly index of 2.42 declined to 1.87 after being run using only important selected features. The depth of the trees generated by various de-cision tree models varied from 1 to 5 branches. The number of peer groups in clustering models was reduced significantly (p

Keywords

Bioinformatics; Modeling; Protein; Halophilic; Halolysin