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Title: Crystallizing Transmembrane Peptides in Lipidic Mesophases

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 {le}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.

Authors:
; ;  [1]
  1. (Trinity)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
FOREIGNNIH
OSTI Identifier:
1023040
Resource Type:
Journal Article
Journal Name:
Biophys. J.
Additional Journal Information:
Journal Volume: 99; Journal Issue: (3) ; 08, 2010; Journal ID: ISSN 0006-3495
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CRYSTALLOGRAPHY; CRYSTALLIZATION; FLEXIBILITY; HYPOTHESIS; MEMBRANE PROTEINS; MEMBRANES; PEPTIDES; PROTEINS; TARGETS

Citation Formats

Höfer, Nicole, Aragão, David, and Caffrey, Martin. Crystallizing Transmembrane Peptides in Lipidic Mesophases. United States: N. p., 2011. Web. doi:10.1016/j.bpj.2010.05.011.
Höfer, Nicole, Aragão, David, & Caffrey, Martin. Crystallizing Transmembrane Peptides in Lipidic Mesophases. United States. doi:10.1016/j.bpj.2010.05.011.
Höfer, Nicole, Aragão, David, and Caffrey, Martin. Wed . "Crystallizing Transmembrane Peptides in Lipidic Mesophases". United States. doi:10.1016/j.bpj.2010.05.011.
@article{osti_1023040,
title = {Crystallizing Transmembrane Peptides in Lipidic Mesophases},
author = {Höfer, Nicole and Aragão, David and Caffrey, Martin},
abstractNote = {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 {le}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.},
doi = {10.1016/j.bpj.2010.05.011},
journal = {Biophys. J.},
issn = {0006-3495},
number = (3) ; 08, 2010,
volume = 99,
place = {United States},
year = {2011},
month = {9}
}