Chapter 6 Forster Resonance Energy Transfer Measurements of Transmembrane Helix Dimerization Energetics

Merzlyakov Mikhail, Hristova Kalina

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Lateral interactions between hydrophobic transmembrane (TM) helices in membranes underlie the folding of multispan membrane proteins and signal transduction by receptor tyrosine kinases (RTKs). Quantitative measurements of dimerization energetics in membranes are required to uncover the physical principles behind these processes. Here, we overview how FRET measurements can be used to determine the thermodynamics of TM helix homo- and heterodimerization in vesicles and in supported bilayers. Such measurements can shed light on the molecular mechanism behind pathologies arising due to single-amino acid mutations in membrane proteins.

Original languageEnglish (US)
Title of host publicationFluorescence Spectroscopy
EditorsLudwig Brand, Michael Johnson
Pages107-127
Number of pages21
DOIs
StatePublished - Dec 1 2008

Publication series

NameMethods in Enzymology
Volume450
ISSN (Print)0076-6879

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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  • Cite this

    Mikhail, M., & Kalina, H. (2008). Chapter 6 Forster Resonance Energy Transfer Measurements of Transmembrane Helix Dimerization Energetics. In L. Brand, & M. Johnson (Eds.), Fluorescence Spectroscopy (pp. 107-127). (Methods in Enzymology; Vol. 450). https://doi.org/10.1016/S0076-6879(08)03406-X