期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 28, 期 10, 页码 445-450出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzv021
关键词
membrane proteins; NMR spectroscopy; phage display; protein domains; proteolysis
资金
- MRC [MC_U105184326] Funding Source: UKRI
- Medical Research Council [MC_U105184326] Funding Source: researchfish
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.
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