Staff Members - Benha University
2. Characterization of lipodisc nanoparticles containing sensory rhodopsin II and its cognate transducer from Natronomonas pharaonic.
Biofizika • 2016
Publication Information
Authors
D. V. Bagrova, *, N. Voskoboynikovab, **, G. A. Armeeva, W. Mosslehyb, G. S. Gluhova, T. T. Ismagulovaa, A. Y. Mulkidjanianb
, M. P. Kirpichnikova, H.-J. Steinhoffb, and K. V. Shaitana.
Keywords
membrane proteins, rhodopsin, lipodisc nanoparticles, transmission electron microscopy, atomic
force microscopy
Journal
Biofizika
Publisher
Pleiades Publishing
Volume
61
Issue
6
Pages
1139-1148
publication.type
International
Paper Link
Not Available
Supplementary Materials
Not Available
Abstract
We describe the preparation and properties of lipodisc nanoparticles – lipid membrane fragments
with a diameter of about 10 nm, stabilized by amphiphilic synthetic polymer molecules. We used the lipodisc
nanoparticles made of Escherichia coli polar lipids and compared lipodisc nanoparticles that contained the
photosensitive protein complex of the sensory rhodopsin with its cognate transducer from the halobacterium
Natronomonas pharaonis with empty lipodisc nanoparticles that contained no protein. The lipodisc nanoparticles were characterized by dynamic light scattering, transmission electron microscopy and atomic force
microscopy. We found that the diameter of lipodisc nanoparticles was not affected by incorporation of the
protein complexes, which makes them a prospective platform for single-molecule studies of membrane proteins.
with a diameter of about 10 nm, stabilized by amphiphilic synthetic polymer molecules. We used the lipodisc
nanoparticles made of Escherichia coli polar lipids and compared lipodisc nanoparticles that contained the
photosensitive protein complex of the sensory rhodopsin with its cognate transducer from the halobacterium
Natronomonas pharaonis with empty lipodisc nanoparticles that contained no protein. The lipodisc nanoparticles were characterized by dynamic light scattering, transmission electron microscopy and atomic force
microscopy. We found that the diameter of lipodisc nanoparticles was not affected by incorporation of the
protein complexes, which makes them a prospective platform for single-molecule studies of membrane proteins.