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Ex vivo stability is a valuable protein characteristic but is laborious to improve experimentally. In addition to biopharmaceutical and industrial applications, stable protein is important for biochemical and structural studies. Taking advantage of the large number of available genomic sequences and growth temperature data, we present two bioinformatic methods to identify a limited set of amino acids or positions that likely underlie thermostability. Because these methods allow thousands of homologs to be examined in silico, they have the advantage of providing both speed and statistical power. Using these methods, we introduced, via mutation, amino acids from thermoadapted homologs into an exemplar mesophilic membrane protein, and demonstrated significantly increased thermostability while preserving protein activity.

Original publication

DOI

10.1016/j.bpj.2015.07.026

Type

Journal article

Journal

Biophys J

Publication Date

06/10/2015

Volume

109

Pages

1420 - 1428

Keywords

Amino Acids, Anti-Bacterial Agents, Antiporters, Bacillus subtilis, Bacterial Proteins, Computational Biology, Escherichia coli, Green Fluorescent Proteins, Mutation, Protein Stability, Temperature, Tetracycline, Transfection