Optimized electrostatic surfaces parallel increased thermostability: a structural bioinformatic analysis
نویسندگان
چکیده
منابع مشابه
Optimized electrostatic surfaces parallel increased thermostability: a structural bioinformatic analysis.
It has been known for some time that thermophilic proteins generally have increased numbers of non-covalent interactions (salt bridges, hydrogen bonds, etc.) compared with their mesophilic orthologs. Recently, anecdotal structural comparisons suggest that non-specific acid-base ion pairs on the protein surface can be an evolutionary efficient mechanism to increase thermostability. In this compr...
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Studies of the structural basis of protein thermostability have produced a confusing picture. Small sets of proteins have been analyzed from a variety of thermophilic species, suggesting different structural features as responsible for protein thermostability. Taking advantage of the recent advances in structural genomics, we have compiled a relatively large protein structure dataset, which was...
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ژورنال
عنوان ژورنال: Protein Engineering Design and Selection
سال: 2003
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/gzg131