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Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis.

Abstract

We have previously reported a phage display method for the identification of protein domains on a genome-wide scale (shotgun proteolysis). Here we present the solution structure of a fragment of the Escherichia coli membrane protein yrfF, as identified by shotgun proteolysis, and determined by NMR spectroscopy. Despite the absence of computational predictions, the fragment formed a well-defined beta-barrel structure, distantly falling within the OB-fold classification. Our results highlight the potential of high-throughput experimental approaches for the identification of protein domains for structural studies.

Type Journal
Authors Allen, M. D.; Christie, M.; Jones, P.; Porebski, B. T.; Roome, B.; Freund, S. M.; Buckle, A. M.; Bycroft, M.; Christ, D.;
Responsible Garvan Author A/Prof Daniel Christ
Publisher Name PROTEIN ENGINEERING DESIGN & SELECTION
Published Date 2015-10-01
Published Volume 28
Published Issue 10
Published Pages 445-50
Status Published in-print
URL link to publisher's version http://www.ncbi.nlm.nih.gov/pubmed/25877662
OpenAccess link to author's accepted manuscript version https://publications.gimr.garvan.org.au/open-access/12771