Time-Resolved Fluorescence Spectroscopy Measures Clustering and Mobility of a G Protein-Coupled Receptor Opsin in Live Cell Membranes | Zendy

William D. Comar | Zendy; Sarah M. Schubert | Zendy; Beata Jastrzȩbska | Zendy; Krzysztof Palczewski | Zendy; Adam W. Smith | Zendy

Open Access

Time-Resolved Fluorescence Spectroscopy Measures Clustering and Mobility of a G Protein-Coupled Receptor Opsin in Live Cell Membranes

Author(s) -

William D. Comar,

Sarah M. Schubert,

Beata Jastrzȩbska,

Krzysztof Palczewski,

Adam W. Smith

Publication year - 2014

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja501948w

Subject(s) - chemistry , opsin , fluorescence spectroscopy , membrane , monomer , biophysics , protein quaternary structure , fluorescence correlation spectroscopy , spectroscopy , fluorescence , population , dimer , equilibrium constant , cell membrane , force spectroscopy , crystallography , photochemistry , molecule , rhodopsin , biochemistry , organic chemistry , optics , polymer , retinal , physics , quantum mechanics , biology , demography , protein subunit , sociology , gene

Determining membrane protein quaternary structure is extremely challenging, especially in live cell membranes. We measured the oligomerization of opsin, a prototypical G protein-coupled receptor with pulsed-interleaved excitation fluorescence cross-correlation spectroscopy (PIE-FCCS). Individual cell measurements revealed that opsin is predominantly organized into dimeric clusters. At low concentrations, we observed that the population of oligomers increased linearly with the square of the individual monomer populations. This finding supports a monomer-dimer equilibrium and provides an experimental measurement of the equilibrium constant.

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