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@ARTICLE{Kriegsmann:5165,
author = {Kriegsmann, J. and Gregor, I. and von der Hocht, I. and
Klare, J. and Engelhard, M. and Enderlein, J. and Fitter,
J.},
title = {{T}ranslational {D}iffusion and {I}nteraction of a
{P}hotoreceptor and {I}ts {C}ognate {T}ransducer {O}bserved
in {G}iant {U}nilamellar {V}esicles by {U}sing
{D}ual-{F}ocus {FCS}},
journal = {ChemBioChem},
volume = {10},
issn = {1439-4227},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {PreJuSER-5165},
pages = {1823 - 1829},
year = {2009},
note = {The priority program SPP 7128 of Deutsche
Forschungsgemeinschaft (F1 84113-1,2 to J.F and to J.E) and
the DFG graduate school 1035 "Biointerface" are acknowledged
for funding. We thank B. Kaupp and G. Baldt for continuous
support in their institutes.},
abstract = {In order to monitor membrane-protein binding in lipid
bilayers at physiological protein concentrations, we
employed the recently developed dual-focus fluorescence
correlation spectroscopy (2fFCS) technique. In a case study
on a photoreceptor consisting of seven transmembrane helices
and its cognate transducer (two transmembrane helices), the
lateral diffusion for these integral membrane proteins was
analyzed in giant unilamellar vesicles (GUVs). The
two-dimensional diffusion coefficients of both separately
diffusing proteins differ significantly, with D = 2.2 x
10(-8) cm2 s(-1) for the photoreceptor and with D = 4.1 x
10(-8) cm2 s(-1) for the transducer. In GUVs with both
membrane proteins present together, we observed
significantly smaller diffusion coefficients for labelled
transducer molecules; this indicates the presence of larger
diffusing units and therefore intermolecular protein
binding. Based on the phenomenological dependence of
diffusion coefficients on the molecule's cylindrical radius,
we are able to estimate the degree of membrane protein
binding on a quantitative level.},
keywords = {Archaeal Proteins: chemistry / Archaeal Proteins:
metabolism / Carotenoids: chemistry / Carotenoids:
metabolism / Diffusion / Lipid Bilayers: chemistry /
Membrane Proteins: chemistry / Photoreceptors, Microbial:
chemistry / Photoreceptors, Microbial: metabolism / Protein
Binding / Spectrometry, Fluorescence / Unilamellar
Liposomes: chemistry / Archaeal Proteins (NLM Chemicals) /
HtrII protein, Natronobacterium pharaonis (NLM Chemicals) /
Lipid Bilayers (NLM Chemicals) / Membrane Proteins (NLM
Chemicals) / Photoreceptors, Microbial (NLM Chemicals) /
Unilamellar Liposomes (NLM Chemicals) / phototaxis receptor
sensory rhodopsin II, Natronobacterium pharaonis (NLM
Chemicals) / Carotenoids (NLM Chemicals) / J (WoSType)},
cin = {ISB-2},
ddc = {540},
cid = {I:(DE-Juel1)ISB-2-20090406},
pnm = {Programm Biosoft},
pid = {G:(DE-Juel1)FUEK443},
shelfmark = {Biochemistry $\&$ Molecular Biology / Chemistry, Medicinal},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19551796},
UT = {WOS:000268504500015},
doi = {10.1002/cbic.200900251},
url = {https://juser.fz-juelich.de/record/5165},
}