Multiple interactions in protein-membrane binding

被引:0
|
作者
Ramsden, JJ [1 ]
机构
[1] Univ Basel, Bioctr, Dept Biophys Chem, CH-4056 Basel, Switzerland
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暂无
中图分类号
TM [电工技术]; TN [电子技术、通信技术];
学科分类号
0808 ; 0809 ;
摘要
The myristoylated-alanine-rich C-kinase substrate (MARCKS) protein is an example of a protein with an indefinite native conformation which can participate in multiple binding interactions with surfaces. It is considered as a paradigm for biomolecules interacting with electronic interfaces in electrooptical devices. An approach to theoretically predicting the interfacial interactions is outlined, and its present limitations delineated. Precision optical waveguide lightmode spectroscopy (OWLS) is used to directly measure the kinetics of association and dissociation to lipid-coated metal oxide surfaces mimicking (for example) a FET gate or an optical modulator.
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页码:244 / 269
页数:26
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