Regulation of Channel Function Due to Coupling with a Lipid Bilayer

被引:14
作者
Ashrafuzzaman, Md [1 ,2 ]
Tuszynski, J. [1 ,3 ]
机构
[1] Univ Alberta, Cross Canc Inst, Dept Oncol, Edmonton, AB T6G 1Z2, Canada
[2] Cornell Univ, Weill Med Coll, Dept Physiol & Biophys, New York, NY 10065 USA
[3] Univ Alberta, Dept Phys, Edmonton, AB T6G 2E1, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Lipid Bilayer; Ion Channel; Membrane Protein; Screened Coulomb Interaction; X-RAY-DIFFRACTION; GRAMICIDIN CHANNEL; PHOSPHOLIPID-BILAYER; INTRINSIC CURVATURE; MEMBRANE-PROTEIN; DEFORMATIONS; ALAMETHICIN; ENERGETICS; POLYELECTROLYTES; CONDUCTANCE;
D O I
10.1166/jctn.2012.2062
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Regulation of membrane protein functions due to hydrophobic coupling with a lipid bilayer is investigated. An energy formula based on the screened Coulomb interaction approximation has been developed between lipid bilayer and integral ion channels with different structures. We find that the hydrophobic bilayer thickness channel length mismatch induces channel destabilization exponentially while negative lipid curvature linearly. Experimental parameters related to channel dynamics are consistent with theoretical predictions. This study provides a new insight that provides better understanding of the underlying mechanisms of membrane protein functions in biological systems.
引用
收藏
页码:564 / 570
页数:7
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