Lipid tail chain asymmetry and the strength of membrane-induced interactions between membrane proteins

Biochimica et Biophysica Acta - Biomembranes

Volumn 1768, Issue 10, 2007, Pages 2393-2399

  Dan, Nily ^a  

^a Drexel University   (United States)

Author keywords

Area modulus; Bending modulus; Transmembrane protein

Indexed keywords

LIPID; MEMBRANE PROTEIN;

ARTICLE; ENERGY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION;

MEMBRANE LIPIDS; MEMBRANE PROTEINS; MEMBRANES;

EID: 34948881202     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.05.003     Document Type: Article

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24. Note that changing the degree of chain saturation (for a fixed number of carbons) is known to affect the surface area per lipid (see, for example, Illya [4] and Niemela [6]). In our model, the thickness of a bilayer composed of saturated 16:16 or 14:18 lipids should be the same, in agreement with previous work [e.g. 4]. However, since introducing an unsaturated bond changes the surface area, the thickness may change as well. As a result, the thickness of a bilayer composed of two saturated 16:16 lipid chains would differ from that of a 16:16 lipid with an unsaturated bond, as shown, for example, by Rawicz et al. [7].