Wave-number Selection by Target Patterns and Side Walls in Rayleigh-Benard Convection

We present experimental results for Rayleigh-Benard convection patterns in a cylindrical container with static side-wall forcing induced by a heater. This forcing stabilized a pattern of concentric rolls (a target pattern) with the central roll (the umbilicus) at the center of the cell after a jump from the conduction to the convection state. A quasi-static increase of the control parameter (epsilon) beyond 0.8 caused the umbilicus of the pattern to move off center. As observed by others, a further quasi-static increase of epsilon up to 15.6 caused a sequence of transitions. Each transition began with the displacement of the umbilicus and then proceeded with the loss of one convection roll at the umbilicus and the return of the umbilicus to a location near the center of the cell. Alternatively, with decreasing epsilon new rolls formed at the umbilicus but large umbilicus displacements did not occur. In addition to quantitative measurements of the umbilicus displacement, we determined and analyzed the entire wave-director field of each image. The wave numbers varied in the axial direction, with minima at the umbilicus and at the cell wall and a maximum at a radial position close to 2/3 Gamma. The wave numbers at the maximum showed hysteretic jumps at the transitions, but on average agreed well with the theoretical predictions for the wave numbers selected in the far field of an infinitely extended target pattern.Comment: ReVTeX, 11 pages, 16 eps figures include

The Domain Chaos Puzzle and the Calculation of the Structure Factor and Its Half-Width

The disagreement of the scaling of the correlation length xi between experiment and the Ginzburg-Landau (GL) model for domain chaos was resolved. The Swift-Hohenberg (SH) domain-chaos model was integrated numerically to acquire test images to study the effect of a finite image-size on the extraction of xi from the structure factor (SF). The finite image size had a significant effect on the SF determined with the Fourier-transform (FT) method. The maximum entropy method (MEM) was able to overcome this finite image-size problem and produced fairly accurate SFs for the relatively small image sizes provided by experiments. Correlation lengths often have been determined from the second moment of the SF of chaotic patterns because the functional form of the SF is not known. Integration of several test functions provided analytic results indicating that this may not be a reliable method of extracting xi. For both a Gaussian and a squared SH form, the correlation length xibar=1/sigma, determined from the variance sigma^2 of the SF, has the same dependence on the control parameter epsilon as the length xi contained explicitly in the functional forms. However, for the SH and the Lorentzian forms we find xibar ~ xi^1/2. Results for xi determined from new experimental data by fitting the functional forms directly to the experimental SF yielded xi ~ epsilon^-nu} with nu ~= 1/4 for all four functions in the case of the FT method, but nu ~= 1/2, in agreement with the GL prediction, in the the case of the MEM. Over a wide range of epsilon and wave number k, the experimental SFs collapsed onto a unique curve when appropriately scaled by xi.Comment: 15 pages, 26 figures, 1 tabl

Characterization of anisotropic nano-particles by using depolarized dynamic light scattering in the near field

Light scattering techniques are widely used in many fields of condensed and sof t matter physics. Usually these methods are based on the study of the scattered light in the far field. Recently, a new family of near field detection schemes has been developed, mainly for the study of small angle light scattering. These techniques are based on the detection of the light intensity near to the sample, where light scattered at different directions overlaps but can be distinguished by Fourier transform analysis. Here we report for the first time data obtained with a dynamic near field scattering instrument, measuring both polarized and depolarized scattered light. Advantages of this procedure over the traditional far field detection include the immunity to stray light problems and the possibility to obtain a large number of statistical samples for many different wave vectors in a single instantaneous measurement. By using the proposed technique we have measured the translational and rotational diffusion coefficients of rod-like colloidal particles. The obtained data are in very good agreement with the data acquired with a traditional light scattering apparatus.Comment: Published in Optics Express. This version has changes in bibliograph

Virus assembly occurs following a pH- or Ca2+-triggered switch in the thermodynamic attraction between structural protein capsomeres

Viral self-assembly is of tremendous virological and biomedical importance. Although theoretical and crystallographic considerations suggest that controlled conformational change is a fundamental regulatory mechanism in viral assembly, direct proof that switching alters the thermodynamic attraction of self-assembling components has not been provided. Using the VP1 protein of polyomavirus, we report a new method to quantitatively measure molecular interactions under conditions of rapid protein self-assembly. We show, for the first time, that triggering virus capsid assembly through biologically relevant changes in Ca2+ concentration, or pH, is associated with a dramatic increase in the strength of protein molecular attraction as quantified by the second virial coefficient (B22). B22 decreases from −2.3 × 10−4 mol ml g−2 (weak protein–protein attraction) to −2.4 × 10−3 mol ml g−2 (strong protein attraction) for metastable and Ca2+-triggered self-assembling capsomeres, respectively. An assembly-deficient mutant (VP1CΔ63) is conversely characterized by weak protein–protein repulsion independently of chemical change sufficient to cause VP1 assembly. Concomitant switching of both VP1 assembly and thermodynamic attraction was also achieved by in vitro changes in ammonium sulphate concentration, consistent with protein salting-out behaviour. The methods and findings reported here provide new insight into viral assembly, potentially facilitating the development of new antivirals and vaccines, and will open the way to a more fundamental physico-chemical description of complex protein self-assembly systems