AFM force measurements on microtubule-associated proteins: the projection domain exerts a long-range repulsive force

被引:67
作者
Mukhopadhyay, R
Hoh, JH
机构
[1] Johns Hopkins Univ, Sch Med, Dept Physiol, Baltimore, MD 21205 USA
[2] Johns Hopkins Univ, Dept Chem Engn, Baltimore, MD 21218 USA
关键词
unstructured; entropic exclusion; microtubule-associated protein 2; tau;
D O I
10.1016/S0014-5793(01)02844-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Microtubule-associated proteins (MAPs) are thought to control spacing between microtubules. We propose that the projection domain is largely unstructured and exerts a long-range repulsive force that is predominantly entropic in origin, providing a physical mechanism for maintaining spacing. To test this hypothesis, we developed an experimental system where MAN are electrostatically end-attached to a flat surface, such that the projection domains extend away from the surface. Atomic force microscopy force measurements on this system show that projection domains exert a long-range (> 100 nm) repulsive force. This force depends on the ionic strength of the solution in a way that is consistent with a polyelectrolyte polymer brush. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:374 / 378
页数:5
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