Stability of halophilic proteins: from dipeptide attributes to discrimination classifier.

Abstract:

:To investigate the molecular features responsible for protein halophilicity is of great significance for understanding the structure basis of protein halo-stability and would help to develop a practical strategy for designing halophilic proteins. In this work, we have systematically analyzed the dipeptide composition of the halophilic and non-halophilic protein sequences. We observed the halophilic proteins contained more DA, RA, AD, RR, AP, DD, PD, EA, VG and DV at the expense of LK, IL, II, IA, KK, IS, KA, GK, RK and AI. We identified some macromolecular signatures of halo-adaptation, and thought the dipeptide composition might contain more information than amino acid composition. Based on the dipeptide composition, we have developed a machine learning method for classifying halophilic and non-halophilic proteins for the first time. The accuracy of our method for the training dataset was 100.0%, and for the 10-fold cross-validation was 93.1%. We also discussed the influence of some specific dipeptides on prediction accuracy.

journal_name

Int J Biol Macromol

authors

Zhang G,Huihua G,Yi L

doi

10.1016/j.ijbiomac.2012.10.031

subject

Has Abstract

pub_date

2013-02-01 00:00:00

pages

1-6

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(12)00428-X

journal_volume

53

pub_type

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