Thermodynamic competition between membrane protein oligomeric states

Self-assembly of protein monomers into distinct membrane protein oligomers provides a general mechanism for diversity in the molecular architectures, and resulting biological functions, of membrane proteins. We develop a general physical framework describing the thermodynamic competition between dif...

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Bibliographic Details
Published inEurophysics letters Vol. 116; no. 2; p. 28005
Main Authors Kahraman, Osman, Haselwandter, Christoph A.
Format Journal Article
LanguageEnglish
Published Les Ulis EDP Sciences, IOP Publishing and Società Italiana di Fisica 01.10.2016
IOP Publishing
Subjects
87.15.kt
87.16.D
87.16.Vy
Biological effects
Cell membranes
Competition
Control
Lipids
Mathematical models
Membranes
Molecular structure
Monomers
Proteins
Self assembly
Thermodynamics
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Summary:Self-assembly of protein monomers into distinct membrane protein oligomers provides a general mechanism for diversity in the molecular architectures, and resulting biological functions, of membrane proteins. We develop a general physical framework describing the thermodynamic competition between different oligomeric states of membrane proteins. Using the mechanosensitive channel of large conductance as a model system, we show how the dominant oligomeric states of membrane proteins emerge from the interplay of protein concentration in the cell membrane, protein-induced lipid bilayer deformations, and direct monomer-monomer interactions. Our results suggest general physical mechanisms and principles underlying regulation of protein function via control of membrane protein oligomeric state.
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publisher-ID:epl18212
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0295-5075
1286-4854
DOI:10.1209/0295-5075/116/28005