scholarly journals 1P086 Structure and Function of Dihydrofolate Reductases from Deep-sea Bacteria(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S168
Author(s):  
Chiho Murakami ◽  
Eiji Ohmae ◽  
Kunihiko Gekko ◽  
Shin-ichi Tate ◽  
Kaoru Nakasone ◽  
...  
Keyword(s):  
Deep Sea ◽  
Protein Function ◽  
Poster Session ◽  
Structure And Function ◽  
Meeting Program ◽  
Deep Sea Bacteria ◽  
Dihydrofolate Reductases ◽  
And Function

scholarly journals 1P076 Molecular basis for recognition of E-cadherin by killer cell-lectin like receptor, KLRG1(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S165
Author(s):  
Seiko Nakamura ◽  
Kimiko Kuroki ◽  
Izuru Ohki ◽  
Kaori Sasaki ◽  
Takuma Maruyama ◽  
...  
Keyword(s):  
Protein Function ◽  
Molecular Basis ◽  
Poster Session ◽  
Killer Cell ◽  
Meeting Program ◽  
E Cadherin

scholarly journals 1P074 Non-native structure of α-lactalbumin-fatty acid complex as an apoptosis induction factor(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S165
Author(s):  
Tatsuro Kamijima ◽  
Toshiya Sato ◽  
Kaoru Akimoto ◽  
Tomoyasu Aizawa ◽  
Keiichi Kawano ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Protein Function ◽  
Poster Session ◽  
Apoptosis Induction ◽  
Native Structure ◽  
Acid Complex ◽  
Meeting Program

scholarly journals Reconstitution of the membrane protein OmpF into biomimetic block copolymer–phospholipid hybrid membranes

2016 ◽  
Vol 7 ◽  
pp. 881-892 ◽  
Author(s):  
Matthias Bieligmeyer ◽  
Franjo Artukovic ◽  
Stephan Nussberger ◽  
Thomas Hirth ◽  
Thomas Schiestel ◽  
...  
Keyword(s):  
Block Copolymers ◽  
Membrane Protein ◽  
Protein Function ◽  
Transmembrane Proteins ◽  
Synthetic Polymer ◽  
Structure And Function ◽  
Membrane Thickness ◽  
Channel Conductance ◽  
Biomimetic Polymer ◽  
And Function

Structure and function of many transmembrane proteins are affected by their environment. In this respect, reconstitution of a membrane protein into a biomimetic polymer membrane can alter its function. To overcome this problem we used membranes formed by poly(1,4-isoprene-block-ethylene oxide) block copolymers blended with 1,2-diphytanoyl-sn-glycero-3-phosphocholine. By reconstituting the outer membrane protein OmpF from Escherichia coli into these membranes, we demonstrate functionality of this protein in biomimetic lipopolymer membranes, independent of the molecular weight of the block copolymers. At low voltages, the channel conductance of OmpF in 1 M KCl was around 2.3 nS. In line with these experiments, integration of OmpF was also revealed by impedance spectroscopy. Our results indicate that blending synthetic polymer membranes with phospholipids allows for the reconstitution of transmembrane proteins under preservation of protein function, independent of the membrane thickness.

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