Measuring the energetics of membrane protein dimerization in mammalian membranes

Lirong Chen, Lawrence Novicky, Mikhail Merzlyakov, Tihomir Hristov, Kalina A Hristova

Research output: Contribution to journalArticle

Abstract

Thus far, quantitative studies of lateral protein interactions in membranes have been restricted peptides or simplified protein constructs in lipid vesicles or bacterial membranes. Here we show how free energies of membrane protein dimerization can be measured in mammalian plasma membrane-derived vesicles. The measurements, performed in single vesicles, utilize the quantitative imaging FRET (Ql-FRET) method. The experiments are described in a step-by-step protocol. The protein characterized is the transmembrane domain of glycophorin A, the most extensively studied membrane protein, known to form homodimers in hydrophobic environments. The results suggest that molecular crowding in cellular membranes has a dramatic effect on the strength of membrane protein interactions. 10.1021/ja910692u

Original languageEnglish (US)
Pages (from-to)3628-3635
Number of pages8
JournalJournal of the American Chemical Society
Volume132
Issue number10
DOIs
StatePublished - Mar 17 2010

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Protein Multimerization
Dimerization
Membrane Proteins
Proteins
Membranes
Glycophorin
Cell membranes
Free energy
Cell Membrane
Lipids
Imaging techniques
Peptides
Experiments

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Measuring the energetics of membrane protein dimerization in mammalian membranes. / Chen, Lirong; Novicky, Lawrence; Merzlyakov, Mikhail; Hristov, Tihomir; Hristova, Kalina A.

In: Journal of the American Chemical Society, Vol. 132, No. 10, 17.03.2010, p. 3628-3635.

Research output: Contribution to journalArticle

Chen, Lirong ; Novicky, Lawrence ; Merzlyakov, Mikhail ; Hristov, Tihomir ; Hristova, Kalina A. / Measuring the energetics of membrane protein dimerization in mammalian membranes. In: Journal of the American Chemical Society. 2010 ; Vol. 132, No. 10. pp. 3628-3635.
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