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

Citation
R. Mukhopadhyay et Jh. Hoh, AFM force measurements on microtubule-associated proteins: the projection domain exerts a long-range repulsive force, FEBS LETTER, 505(3), 2001, pp. 374-378
Citations number
36
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
505
Issue
3
Year of publication
2001
Pages
374 - 378
Database
ISI
SICI code
0014-5793(20010921)505:3<374:AFMOMP>2.0.ZU;2-2
Abstract
Microtubule-associated proteins (MAPs) are thought to control spacing betwe en microtubules. We propose that the projection domain is largely unstructu red 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 electros tatically 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) rep ulsive force. This force depends on the ionic strength of the solution in a way that is consistent with a polyelectrolyte polymer brush. (C) 2001 Publ ished by Elsevier Science B.V. on behalf of the Federation of European Bioc hemical Societies.