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2017 ; 7
(1
): 12000
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New views on phototransduction from atomic force microscopy and single molecule
force spectroscopy on native rods
#MMPMID28931892
Maity S
; Ilieva N
; Laio A
; Torre V
; Mazzolini M
Sci Rep
2017[Sep]; 7
(1
): 12000
PMID28931892
show ga
By combining atomic force microscopy (AFM) imaging and single-molecule force
spectroscopy (SMFS), we analyzed membrane proteins of the rod outer segments
(OS). With this combined approach we were able to study the membrane proteins in
their natural environment. In the plasma membrane we identified native cyclic
nucleotide-gated (CNG) channels which are organized in single file strings. We
also identified rhodopsin located both in the discs and in the plasma membrane.
SMFS reveals strikingly different mechanical properties of rhodopsin unfolding in
the two environments. Molecular dynamic simulations suggest that this difference
is likely to be related to the higher hydrophobicity of the plasma membrane, due
to the higher cholesterol concentration. This increases rhodopsin mechanical
stability lowering the rate of transition towards its active form, hindering, in
this manner, phototransduction.