一种设计的跨膜肽的结合协同性与特异性。
Cooperativity and specificity of association of a designed transmembrane peptide.
作者信息
Gratkowski Holly, Dai Qing-Hong, Wand A Joshua, DeGrado William F, Lear James D
机构信息
The Johnson Research foundation, Department of Biochemistry and University of Pennsylvania, Philadelphia PA 19104-6059, USA.
出版信息
Biophys J. 2002 Sep;83(3):1613-9. doi: 10.1016/S0006-3495(02)73930-1.
Abstract
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.
摘要
旨在定量表征氨基酸取代自由能效应的热力学研究并不局限于双态系统，但确实需要知道所考虑平衡中涉及的状态数。通过分析超速离心和核磁共振方法，我们在此表明，通过修饰水溶性卷曲螺旋GCN4-P1的序列设计的膜溶性肽MS1，在去污剂胶束中表现出可逆的单体-二聚体-三聚体缔合，在C14-甜菜碱中比在十二烷基磷酸胆碱去污剂中具有更高的协同程度。
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