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 language | English (US) |
|---|---|
| Title of host publication | Fluorescence Spectroscopy |
| Editors | Ludwig Brand, Michael Johnson |
| Pages | 107-127 |
| Number of pages | 21 |
| DOIs | |
| State | Published - Dec 1 2008 |
Publication series
| Name | Methods in Enzymology |
|---|---|
| Volume | 450 |
| 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