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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

SUBMITTER: Hofer N 

PROVIDER: S-EPMC2913208 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Crystallizing transmembrane peptides in lipidic mesophases.

Höfer Nicole N   Aragão David D   Caffrey Martin M  

Biophysical journal 20100801 3


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,  ...[more]

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