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research article

Pre-transition effects mediate forces of assembly between transmembrane proteins

Katira, Shachi
•
Mandadapu, Kranthi K.
•
Vaikuntanathan, Suriyanarayanan
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2016
Elife

We present a mechanism for a generic, powerful force of assembly and mobility for transmembrane proteins in lipid bilayers. This force is a pre-transition (or pre-melting) effect for the first-order transition between ordered and disordered phases in the membrane. Using large-scale molecular simulation, we show that a protein with hydrophobic thickness equal to that of the disordered phase embedded in an ordered bilayer stabilizes a microscopic order-disorder interface. The stiffness of that interface is finite. When two such proteins approach each other, they assemble because assembly reduces the net interfacial energy. Analogous to the hydrophobic effect, we refer to this phenomenon as the 'orderphobic effect'. The effect is mediated by proximity to the order-disorder phase transition and the size and hydrophobic mismatch of the protein. The strength and range of forces arising from this effect are significantly larger than those that could arise from membrane elasticity for the membranes considered.

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Type
research article
DOI
10.7554/eLife.13150
Web of Science ID

WOS:000373889500001

Author(s)
Katira, Shachi
•
Mandadapu, Kranthi K.
•
Vaikuntanathan, Suriyanarayanan
•
Smit, Berend  
•
Chandler, David
Date Issued

2016

Publisher

Elife Sciences Publications Ltd

Published in
Elife
Volume

5

Article Number

e13150

Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LSMO  
Available on Infoscience
July 19, 2016
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/127499
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