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Computational design of a substrate specificity mutant of a protein

✍ Scribed by Honda, Nobuo; Komeiji, Yuto; Uebayasi, Masami; Yamato, Ichiro

Book ID: 102648404
Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 548 KB
Volume: 26
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199612)26:4<459::aid-prot6>3.0.co;2-6

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✦ Synopsis

The wild-type trp repressor of E. coli bound 5-methoxytryptophan, a Trp analogue, less tightly than Trp. A mutant repressor (Val-+Ala) that should bind 5-methoxytryptophan preferentially to Trp was computationally designed by free-energy calculations accompanied by free-energy decomposition. The designed mutant was demonstrated b y experiments to bind 5-methoxytryptophan more tightly than Trp, consistent with the computational prediction. This success indicates the usefulness of free energy decomposition in protein design.

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