Surfing on Protein Waves: Proteophoresis as a Mechanism for Bacterial Genome Partitioning.

Efficient bacterial chromosome segregation typically requires the coordinated action of a three-component machinery, fueled by adenosine triphosphate, called the partition complex. We present a phenomenological model accounting for the dynamic activity of this system that is also relevant for the physics of catalytic particles in active environments. The model is obtained by coupling simple linear reaction-diffusion equations with a proteophoresis, or "volumetric" chemophoresis, force field that arises from protein-protein interactions and provides a physically viable mechanism for complex translocation. This minimal description captures most known experimental observations: dynamic oscillations of complex components, complex separation, and subsequent symmetrical positioning. The predictions of our model are in phenomenological agreement with and provide substantial insight into recent experiments. From a nonlinear physics view point, this system explores the active separation of matter at micrometric scales with a dynamical instability between static positioning and traveling wave regimes triggered by the dynamical spontaneous breaking of rotational symmetry.

Single-molecule super-resolution imaging in bacteria.

Bacteria have evolved complex, multi-component cellular machineries to carry out fundamental cellular processes such as cell division/separation, locomotion, protein secretion, DNA transcription/replication, or conjugation/competence. Diffraction of light has so far restricted the use of conventional fluorescence microscopy to reveal the composition, internal architecture and dynamics of these important machineries. This review describes some of the more recent advances on single-molecule super-resolution microscopy methods applied to bacteria and highlights their application to chemotaxis, cell division, DNA segregation, and DNA transcription machineries. Finally, we discuss some of the lessons learned from this approach, and future perspectives.

A model for protein-DNA interaction dynamics.

We map a simplified version of the protein-DNA interaction problem into an Ising-model in a random magnetic field. The model includes a "head" which moves along the chain while interacting with the underlying spins. The head moves by using the statistical fluctuations of base openings. A Monte Carlo (MC) simulation of this model reveals the possibility of biased diffusion in one direction, followed by sequence identification and binding. The model provides some insight into the mechanisms used by some repressor proteins to diffuse and bind to specific DNA-binding sites.

Heat does not come in different colours: entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions.

Modern techniques in microcalorimetry allow us to measure directly the heat changes and associated thermodynamics for biomolecular processes in aqueous solution at reasonable concentrations. All these processes involve changes in solvation/hydration, and it is natural to assume that the heats for these processes should reflect, in some way, such changes in solvation. However, the interpretation of data is still somewhat ambiguous, since different non-covalent interactions may have similar thermodynamic signatures, and analysis is frustrated by large entropy-enthalpy compensation effects. Changes in heat capacity (Delta C(p)) have been related to changes in hydrophobic hydration and non-polar accessible surface areas, but more recent empirical and theoretical work has shown how this need not always be the case. Entropy-enthalpy compensation is a natural consequence of finite Delta C(p) values and, more generally, can arise as a result of quantum confinement effects, multiple weak interactions, and limited free energy windows, giving rise to thermodynamic homeostasis that may be of evolutionary and functional advantage. The new technique of pressure perturbation calorimetry (PPC) has enormous potential here as a means of probing solvation-related volumetric changes in biomolecules at modest pressures, as illustrated with preliminary data for a simple protein-inhibitor complex.

Coupling between molecular vibrations and liquid crystalline order parameters.

Specific Raman active modes in two prototype cyanobiphenyl liquid crystals are shown to display a temperature dependent softening proportional to either the nematic or smectic order parameters, while other vibrations (like the C identical withN stretch mode) remain unaltered. This selective coupling between intramolecular vibrations and the liquid crystalline order is related to the intrinsic symmetry of the modes. The method provides a simple, microscopic, noninvasive optical technique with which the liquid crystalline order parameters can be qualitatively mapped out.

Comment on "Photon transmission technique for studying multiple phase transitions in a liquid crystal".

Contrary to the recently published results by Ozbek et al. [Phys. Rev. E 59, 6798 (1999)], we argue that the transmitted light intensity through an unoriented sample is by no means a good measure of the order parameters of the different phase transitions of a liquid crystal.

Phonon self-energies and phase transitions in a prototype discotic liquid crystal

Specific Raman active vibrations in the discotic liquid crystal nematogen hexakis(6-hexyloxy)triphenylene are shown to be sensitive to either the isotropic<-->columnar or the columnar<-->solid phase transitions. Changes in frequency and/or intensity of vibrations with specific symmetries demonstrate that the method can be used not only to monitor the phase transitions themselves with a microscopic and noninvasive optical technique, but also to gain physical information on the origin of the molecular interactions that produce them.

Photoinduced oxygen dynamics in lyophilized hemoglobin.

Reversible laser induced deoxygenation in the lyophilized phase of hemoglobin is demonstrated by means of resonant Raman scattering, luminescence, and optical transmission. Specific Raman modes, which are both sensitive to the spin states of Fe(II) in the hemes and resonant in the visible, are monitored as a function of time to evaluate the effect of the illuminating laser. These modes act as in-situ markers of the oxygen content of the protein. The reversible photoinduced deoxygenation can be observed through both the Raman spin-markers and the optical transmission experiments. In the former, reversible changes in the intensities of specific Raman modes are observed, while in the latter, the oscillator strength of the two main absorptions of oxyhemoglobin in the visible are seen to vary accordingly. The luminescence in lyophilized hemoglobin is found to have at least two different contributions, (i) a resonant component with the Raman modes and; (ii) a nonresonant contribution, which increases at high input laser powers and eventually masks the Raman signals. The nonresonant contribution is the luminescence of the photoproduct achieved by thermal denaturation of the protein and remains standing as a permanent nonreversible damage in the illuminated spot. Semiempirical electronic calculations of the wavefunction and total energy of the iron porphyrin reveal the underlying physical origin of the laser induced deoxygenation process in the hemes and are also presented.

Universal low-frequency vibrations of proteins from a simple interaction potential.

A pairwise Born potential connecting the heavy atom sites within a prescribed cutoff, and the equation of motion method (EOM), reproduce the existence of a universal singularity in the low-frequency vibrational density of states of typical globular proteins. This is due to quasilocalization of acoustic waves and an analogy with a similar feature found in glasses is stressed. We explain the dependence of this anomaly with the effective dimensionality of the protein. The EOM method allows for the study of even the largest proteins with a simple personal computer.