skip to main content

DOE PAGESDOE PAGES

Title: Pre-transition effects mediate forces of assembly between transmembrane proteins

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. Furthermore, 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.
Authors:
 [1] ;  [2] ;  [3] ;  [4] ;  [1]
  1. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Dept. of Chemistry
  2. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Dept. of Chemistry and Dept. of Chemical and Biomolecular Engineering
  3. Univ. of Chicago, IL (United States). Dept. of Chemistry
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Dept. of Chemistry, Chemical Sciences Div.; Ecole Polytechnique Federale Lausanne (Switzlerland). Inst. des Sciences et Ingenierie Chimiques
Publication Date:
Grant/Contract Number:
AC02-05CH11231
Type:
Accepted Manuscript
Journal Name:
eLife
Additional Journal Information:
Journal Volume: 5; Journal Issue: February; Journal ID: ISSN 2050-084X
Publisher:
eLife Sciences Publications, Ltd.
Research Org:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES
OSTI Identifier:
1414748

Katira, Sachi, Mandadapu, Kranthi K., Vaikuntanathan, Suriyanarayanan, Smit, Berend, and Chandler, David. Pre-transition effects mediate forces of assembly between transmembrane proteins. United States: N. p., Web. doi:10.7554/eLife.13150.001.
Katira, Sachi, Mandadapu, Kranthi K., Vaikuntanathan, Suriyanarayanan, Smit, Berend, & Chandler, David. Pre-transition effects mediate forces of assembly between transmembrane proteins. United States. doi:10.7554/eLife.13150.001.
Katira, Sachi, Mandadapu, Kranthi K., Vaikuntanathan, Suriyanarayanan, Smit, Berend, and Chandler, David. 2016. "Pre-transition effects mediate forces of assembly between transmembrane proteins". United States. doi:10.7554/eLife.13150.001. https://www.osti.gov/servlets/purl/1414748.
@article{osti_1414748,
title = {Pre-transition effects mediate forces of assembly between transmembrane proteins},
author = {Katira, Sachi and Mandadapu, Kranthi K. and Vaikuntanathan, Suriyanarayanan and Smit, Berend and Chandler, David},
abstractNote = {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. Furthermore, 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.},
doi = {10.7554/eLife.13150.001},
journal = {eLife},
number = February,
volume = 5,
place = {United States},
year = {2016},
month = {2}
}