LOWER BOUNDS FOR THE BUCKLING PRESSURE OF SPHERICAL SHELLS

Hydrostatic buckling pressure calculations for spherical shell

Bifurcation structures and transient chaos in a four-dimensional Chua model

A four-dimensional four-parameter Chua model with cubic nonlinearity is studied applying numerical continuation and numerical solutions methods. Regarding numerical solution methods, its dynamics is characterized on Lyapunov and isoperiodic diagrams and regarding numerical continuation method, the bifurcation curves are obtained. Combining both methods the bifurcation structures of the model were obtained with the possibility to describe the {\it shrimp}-shaped domains and their endoskeletons. We study the effect of a parameter that controls the dimension of the system leading the model to present transient chaos with its corresponding basin of attraction being riddled.Comment: 9 figures, to appear in PL

VSR symmetries in the DKP algebra: the interplay between Dirac and Elko spinor fields

VSR symmetries are here naturally incorporated in the DKP algebra on the spin-0 and the spin-1 DKP sectors. We show that the Elko (dark) spinor fields structure plays an essential role on accomplishing this aim, unravelling hidden symmetries on the bosonic DKP fields under the action of discrete symmetries.Comment: 17 page

Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU

Hsc66 and Hsc20 comprise a specialized chaperone system important for the assembly of iron-sulfur clusters in Escherchia coli. Only a single substrate, the Fe/S template protein IscU, has been identified for the Hsc66/Hsc20 system, but the mechanism by which Hsc66 selectively binds IscU is unknown. We have investigated Hsc66 substrate specificity using phage display and a peptide array of IscU. Screening of a heptameric peptide phage display library revealed that Hsc66 prefers peptides with a centrally located Pro-Pro motif. Using a cellulose-bound peptide array of IscU we determined that Hsc66 interacts specifically with a region (residues 99-103, LPPVK) that is invariant among all IscU family members. A synthetic peptide (ELPPVKIHC) corresponding to IscU residues 98-106 behaves in a similar manner to native IscU, stimulating the ATPase activity of Hsc66 with similar affinity as IscU, preventing Hsc66 suppression of bovine rhodanese aggregation, and interacting with the peptide-binding domain of Hsc66. Unlike native IscU, however, the synthetic peptide is not bound by Hsc20 and does not synergistically stimulate Hsc66 ATPase activity with Hsc20. Our results indicate that Hsc66 and Hsc20 recognize distinct regions of IscU and further suggest that Hsc66 will not bind LPPVK motifs with high affinity in vivo unless they are in the context of native IscU and can be directed to Hsc66 by Hsc20