| Abstrakt: |
Tubulin, a globular protein, mostly distributed in nature in the dimeric α, β form, can polymerize in vivo and in vitro into microtubules—longitudinal dynamic assemblies, involved in numerous cellular functions, including cell division and signaling. Tubulin polymerization starts upon binding Mg2+ with the tubulin guanosine triphosphate (GTP) site. In the current study we show that a series of repeated femtosecond laser impulses activate the same site without adding Mg2+. GTP site activation (without GTP no polymerization occurs) produces hydrated electrons (they are detected by the UV spectra), which are trapped in the shell of biological water, surrounding the tubulin. These electrons generate an additional, nonlinear by nature, polarization effect, responsible for the second harmonic generation at λ=365 nm (the first harmonic is centered at λ=730 nm) and manyfold increase in strength of the initial electric field. The results are supported by model calculations, based on the assumption of positive (negative) feedback, appearing on interaction of charge transfer exciton dipoles with the applied electromagnetic field. © 2004 American Institute of Physics. [ABSTRACT FROM AUTHOR] |
