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Title: Crystallizing Transmembrane Peptides in Lipidic Mesophases
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Keywords: Biochemistry
membrane proteins
Issue Date: 2010
Citation: Höfer N, Aragão D, Caffrey M, Crystallizing Transmembrane Peptides in Lipidic Mesophases, Biophysical Journal, 99, 3, 2010, L23-L25
Series/Report no.: Biophysical Journal
Abstract: Structure determination of membrane proteins by crystallographic means has been facilitated by crystallization in lipidic mesophases. It has been suggested, however, that this so-called in meso method, as originally implemented, would not apply to small protein targets having ≤4 transmembrane crossings. In our study, the hypothesis that the inherent flexibility of the mesophase would enable crystallogenesis of small proteins was tested using a transmembrane pentadecapeptide, linear gramicidin, which produced structure-grade crystals. This result suggests that the in meso method should be considered as a viable means for high-resolution structure determination of integral membrane peptides, many of which are predicted to be coded for in the human genome.
Description: PUBLISHED
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Access: OpenAccess
Appears in Collections:Biochemistry (Scholarly Publications)

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Crystallizing Transmembrane Peptides in Lipidic Mesophases - supplemental.pdfPublished (author's copy) - Peer Reviewed538.69 kBAdobe PDFView/Open
Crystallizing Transmembrane Peptides in Lipidic Mesophases.pdfPublished (author's copy) - Peer Reviewed189.8 kBAdobe PDFView/Open

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