Cooperativity and specificity of association of a designed transmembrane peptide

被引:24
作者
Gratkowski, H
Dai, QH
Wand, AJ
DeGrado, WF
Lear, JD
机构
[1] Johnson Fdn, Sch Med, Dept Biochem, Philadelphia, PA 19104 USA
[2] Univ Penn, Philadelphia, PA 19104 USA
关键词
D O I
10.1016/S0006-3495(02)73930-1
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Thermodynamics studies aimed at quantitatively characterizing free energy effects of amino acid substitutions are not restricted to two state systems, but do require knowing the number of states involved in the equilibrium under consideration. Using analytical ultracentrifugation and NMR methods, we show here that a membrane-soluble peptide, MS1, designed by modifying the sequence of the water-soluble coiled-coil GCN4-P1, exhibits a reversible monomer-dimer-trimer association in detergent micelles with a greater degree of cooperativity in C14-betaine than in dodecyl phosphocholine detergents.
引用
收藏
页码:1613 / 1619
页数:7
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