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AFM force measurements on microtubule‐associated proteins: the projection domain exerts a long‐range repulsive force
Author(s) -
Mukhopadhyay Rajendrani,
Hoh Jan H.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02844-7
Subject(s) - microtubule , projection (relational algebra) , atomic force microscopy , range (aeronautics) , surface (topology) , domain (mathematical analysis) , surface force , chemical physics , polymer , biophysics , physics , chemistry , classical mechanics , nanotechnology , materials science , geometry , mathematical analysis , nuclear magnetic resonance , mathematics , biology , composite material , algorithm , microbiology and biotechnology
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 MAPs 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.