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Biochimie. 2007 Nov;89(11):1433-7. Epub 2007 Jun 30.

A mutational study of transmembrane helix-helix interactions.

Author information

1
Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Albert-Ludwigs-Universität Freiburg, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany.

Abstract

Diverse methods have been developed and applied in the recent years to study interaction of transmembrane alpha-helices and often interaction of single transmembrane helices is followed on SDS-gels. Here we compare two measurements of the stability of a transmembrane helix-helix interaction, and the stability of the PsbF transmembrane helix dimer was determined in a biological membrane as well as in SDS. The observations described in this study demonstrate that the environment, in which a transmembrane helix interaction is studied, can be very critical and detergent properties can significantly influence transmembrane helix interactions, especially, when the transmembrane domain contains strongly polar residues.

PMID:
17688996
DOI:
10.1016/j.biochi.2007.06.006
[Indexed for MEDLINE]

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