이상욱
2017-09-08T01:34:14Z
2017-09-08T01:34:14Z
2015-11
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, v. 484, Page. 184-189
0927-7757
1873-4359
http://www.sciencedirect.com/science/article/pii/S0927775715301394?via%3Dihub
http://hdl.handle.net/20.500.11754/28973
Integral membrane proteins (IMPS) performing a variety of cell functions comprise a significant fraction of the proteins encoded in an organism's genome. Maltose-neopentyl glycol-3 (MNG-3) was invented as a novel detergent to extract IMPs from the cell membranes; MNG-3 has an inherent flexibility originating from its central carbon and its arms comprising alkyl chains and maltose groups. Herein, we demonstrate the reverse-scissoring behavior of MNG-3 through the use of different subphase conditions at the air/water interface. The origin of its high performance was investigated by means of Langmuir techniques, X-ray reflectivity (XRR) analysis of its Langmuir-Schaefer (LS) film, Brewster angle microscope (BAM) and atomic force microscope (AFM) and computational simulation. (C) 2015 Elsevier B.V. All rights reserved.
This work was supported by the National Research Foundation of Korea (NRF: 2015M2B2A9032029) grant funded by the Korea government (MEST).
en
ELSEVIER SCIENCE BV
Integral membrane proteins
Protein surfactant
MNG-3
Langmuir-Schaefer film
X-ray reflectivity
Surface pressure-area isotherm
Behavior of maltose-neopentyl glycol-3 (MNG-3) at the air/aqueous interface
Article
484
10.1016/j.colsurfa.2015.07.054
184-189
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
Yoo, Bowon
Lee, Jisun
Choi, Soyoung
Ryu, Jungju
Lee, Hoik
Chae, Pil Seok
Lee, Sang Uck
Maeda, Mizuo
Sohn, Daewon
2015002344
S
GRADUATE SCHOOL[S]
DEPARTMENT OF BIONANOTECHNOLOGY
sulee
J-9027-2014
http://orcid.org/0000-0001-9596-2349