Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 358, Issue 1, Pages 1-7Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.01.086
Keywords
heterodimer; FRET; receptor tyrosine kinase; fibroblast growth factor receptor 3; transmembrane domain
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Funding
- NIGMS NIH HHS [R01 GM068619] Funding Source: Medline
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Here, we show that the energetics of transmembrane helix heterodimer formation can be characterized in liposomes using Forster resonance energy transfer (FRET). We present the theory and the protocol for measuring the free energy of heterodimerization, and the total (hetero and homo-dimeric) dimer fraction. We use the presented methodology to determine the propensity for heterodimer formation between wild-type fibroblast growth factor receptor 3 (FGFR3) transmembrane domain and the Ala391Glu mutant, linked to Crouzon syndrome with acanthosis nigricans. (c) 2006 Elsevier Ltd. All rights reserved.
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