Journal
BIOPHYSICAL JOURNAL
Volume 109, Issue 7, Pages 1420-1428Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2015.07.026
Keywords
-
Categories
Funding
- National Institutes of Health [R01-GM093825, R01-DK099023, R01-DK073973, R01-MH083840]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available