أعضاء هيئة التدريس - جامعة بنها
1. Characterization of an archaeal photoreceptor/transducer complex from Natronomonas pharaonis assembled within styrene–maleic acid lipid particles
RSC Advances • 2017
معلومات البحث
المؤلفون
N. Voskoboynikova, †a W. Mosslehy, †a A. Colbasevici, a T. T. Ismagulova, b
D. V. Bagrov, b A. A. Akovantseva, d P. S. Timashev, cd A. Y. Mulkidjanian, a
V. N. Bagratashvili, d K. V. Shaitan, b M. P. Kirpichnikovb and H.-J. Steinhoff.
الكلمات المفتاحية
Not Available
المجلة العلمية
RSC Advances
الناشر
Royal Society of Chemistry
المجلد
7
العدد
51324
الصفحات
Not Available
publication.type
International
رابط البحث
Not Available
المواد المرفقة
Not Available
الملخص
The styrene–maleic acid (SMA) copolymers enable a detergent-free extraction of membrane proteins from
lipid bilayers yielding stable water-soluble nanocontainers with lipid-encased proteins. Here, we
demonstrate the ability of the SMA copolymer to extract a complex of interacting membrane proteins
from proteoliposomes, namely the archaeal sensory rhodopsin II from Natronomonas pharaonis, NpSRII,
in complex with its transducer, NpHtrII. The NpSRII/NpHtrII complexes retained their structural integrity
within SMA lipid particles as revealed by diverse biophysical techniques. Pulse electron paramagnetic
resonance data showed the SMA-encased NpSRII/NpHtrII complexes as native-like 2 : 2 dimers with
a distance between NpSRII sites 159 according to the “V”-shaped conformation found in a crystal structure.
lipid bilayers yielding stable water-soluble nanocontainers with lipid-encased proteins. Here, we
demonstrate the ability of the SMA copolymer to extract a complex of interacting membrane proteins
from proteoliposomes, namely the archaeal sensory rhodopsin II from Natronomonas pharaonis, NpSRII,
in complex with its transducer, NpHtrII. The NpSRII/NpHtrII complexes retained their structural integrity
within SMA lipid particles as revealed by diverse biophysical techniques. Pulse electron paramagnetic
resonance data showed the SMA-encased NpSRII/NpHtrII complexes as native-like 2 : 2 dimers with
a distance between NpSRII sites 159 according to the “V”-shaped conformation found in a crystal structure.