Stochastic Dynamics of Magnetosomes in Cytoskeleton

Rotations of microscopic magnetic particles, magnetosomes, embedded into the cytoskeleton and subjected to the influence of an ac magnetic field and thermal noise are considered. Magnetosome dynamics is shown to comply with the conditions of the stochastic resonance under not-too-tight constraints on the character of the particle's fastening. The excursion of regular rotations attains the value of order of radian that facilitates explaining the biological effects of low-frequency weak magnetic fields and geomagnetic fluctuations. Such 1-rad rotations are effectively controlled by slow magnetic field variations of the order of 200 nT.Comment: LaTeX2e, 7 pages with 3 figure

Classical glueballs in non-Abelian Born-Infeld theory

It is shown that the Born-Infeld-type modification of the quadratic Yang-Mills action suggested by the superstring theory gives rise to classical particle-like solutions prohibited in the standard Yang-Mills theory. This becomes possible due to the scale invariance breaking by the Born-Infeld non-linearity. New classical glueballs are sphaleronic in nature and exhibit a striking similarity with the Bartnik-McKinnon solutions of the Yang-Mills theory coupled to gravity.Comment: Revtex, 4 pages, 2 eps figure

Temperature and pH sensitivity of the O(640) intermediate of the bacteriorhodopsin photocycle

The temperature and pH dependencies of the O(640) intermediate of the photocycle of bacteriorhodopsin (bR) were investigated by flash photolysis and T-jump experiments. The maximal concentration of the O(640) intermediate was found to be dependent on the temperature, which is described by a sigmoidal relationship. With increasing pH the midpoint of the sigmoidal curves shifts to higher temperatures. The Van't Hoff equation provides enthalpy and entropy values of the observed states. These results indicate that, in the investigated temperature (0-60°C) and pH (pH 4.0-10.0) range, the sequence of the principal intermediates in the pathway “M-N-O-bR” does not change. The observations of the O(640) intermediate at pH < 8.0 and of the N(550) intermediate at pH > 8.0 are most probably due only to changes of the intrinsic rate constants of the bR photocycle, not to a different mechanism

Spectrally silent transitions in the bacteriorhodopsin photocycle.

The photocycle kinetics of bacteriorhodopsin were analyzed from 0 to 40 degrees C at 101 wavelengths (330-730 nm). The data can be satisfactorily approximated by eight exponents. The slowest component (half-time 20 ms at 20 degrees C) belongs to the 13-cis cycle. The residual seven exponentials that are sufficient to describe the all-trans photocycle indicate that at least seven intermediates of the all-trans cycle must exist, although only five spectrally distinct species (K, L, M, N, and O) have been identified. These seven exponentials and their spectra at different temperatures provide the basis for the discussion of various kinetic schemes of the relaxation. The simplest model of irreversible sequential transitions includes after the first K--> L step the quasiequilibria of L<-->M, M<-->N, and N<-->O intermediates. These quasiequilibria are controlled by rate-limiting dynamics of the protein and/or proton transfer steps outside the chromophore region. Thus there exists an apparent kinetic paradox (i.e., why is the number of exponents of relaxation (at least seven) higher than the number of distinct spectral intermediates (only five)), which can be explained by assuming that some of the transitions correspond to changes in the quasiequilibria between spectrally distinct intermediates (i.e., are spectrally silent)