Identification of the Hydrophobic Thickness of a Membrane Protein Using Fluorescence Spectroscopy:  Studies with the Mechanosensitive Channel MscL†,1

Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5713-5721 ◽  
Author(s):  
Andrew M. Powl ◽  
J. Neville Wright ◽  
J. Malcolm East ◽  
Anthony G. Lee
Keyword(s):  
Membrane Protein ◽  
Fluorescence Spectroscopy ◽  
Mechanosensitive Channel ◽  
Spectroscopy Studies

scholarly journals Fluorescence spectroscopy studies of HEK293 cells expressing DOR-Gi1α fusion protein; the effect of cholesterol depletion

2011 ◽  
Vol 1808 (12) ◽  
pp. 2819-2829 ◽  
Author(s):  
Jana Brejchová ◽  
Jan Sýkora ◽  
Kateřina Dlouhá ◽  
Lenka Roubalová ◽  
Pavel Ostašov ◽  
...  
Keyword(s):  
Fluorescence Spectroscopy ◽  
Fusion Protein ◽  
Hek293 Cells ◽  
Cholesterol Depletion ◽  
Spectroscopy Studies

scholarly journals Cholesterol-dependent partitioning of PtdIns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa)

2004 ◽  
Vol 379 (3) ◽  
pp. 527-532 ◽  
Author(s):  
Richard M. EPAND ◽  
Phan VUONG ◽  
Christopher M. YIP ◽  
Shohei MAEKAWA ◽  
Raquel F. EPAND
Keyword(s):  
Membrane Protein ◽  
Fluorescence Microscopy ◽  
Fluorescence Spectroscopy ◽  
Membrane Domains ◽  
Domain Formation ◽  
Membrane Domain ◽  
Terminal Fragment ◽  
N Terminus ◽  
Total Internal Reflectance ◽  
Internal Reflectance

A myristoylated peptide corresponding to the N-terminus of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of BODIPY®-TMR-labelled PtdIns(4,5)P2 in bilayers of 1-palmitoyl-2-oleoyl phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY®–PtdIns(4,5)2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy revealed the cholesterol-dependent nature of PtdIns(4,5)P2-enriched membrane-domain formation.

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