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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




Journal article


Biophysical journal

Publication Date





1420 - 1428


Department of Cell Biology, The Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York. Electronic address:


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