Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone.

We report the crystal structure of nuclear import receptor Importin-9 bound to its cargo, the histones H2A-H2B. Importin-9 wraps around the core, globular region of H2A-H2B to form an extensive interface. The nature of this interface coupled with quantitative analysis of deletion mutants of H2A-H2B suggests that the NLS-like sequences in the H2A-H2B tails play a minor role in import. Importin-9•H2A-H2B is reminiscent of interactions between histones and histone chaperones in that it precludes H2A-H2B interactions with DNA and H3-H4 as seen in the nucleosome. Like many histone chaperones, which prevent inappropriate non-nucleosomal interactions, Importin-9 also sequesters H2A-H2B from DNA. Importin-9 appears to act as a storage chaperone for H2A-H2B while escorting it to the nucleus. Surprisingly, RanGTP does not dissociate Importin-9•H2A-H2B but assembles into a RanGTP•Importin-9•H2A-H2B complex. The presence of Ran in the complex, however, modulates Imp9-H2A-H2B interactions to facilitate its dissociation by DNA and assembly into a nucleosome

Path Integral Approach to Strongly Nonlinear Composite

We study strongly nonlinear disordered media using a functional method. We solve exactly the problem of a nonlinear impurity in a linear host and we obtain a Bruggeman-like formula for the effective nonlinear susceptibility. This formula reduces to the usual Bruggeman effective medium approximation in the linear case and has the following features: (i) It reproduces the weak contrast expansion to the second order and (ii) the effective medium exponent near the percolation threshold are $s=1$, $t=1+\kappa$, where $\kappa$ is the nonlinearity exponent. Finally, we give analytical expressions for previously numerically calculated quantities.Comment: 4 pages, 1 figure, to appear in Phys. Rev.

Mesure statistique de la résistance de contact d’une grille sérigraphiée pour cellules solaires au silicium multicristallin

La métallisation par sérigraphie est une des étapes les plus importantes dans la technologie d’élaboration des cellules solaires pour une production à grande échelle. Néanmoins, elle demeure dépendante de plusieurs paramètres variables. Pour le silicium multi cristallin, tout changement dans le procédé de réalisation des cellules solaires influence directement l’optimisation du profil de recuit de la métallisation par sérigraphie. Les plaquettes de silicium multi cristallin subissent toutes les étapes classiques de réalisation des cellules solaires comme le nettoyage chimique et la décontamination, une diffusion au phosphore et le dépôt du nitrure de silicium SiNx par PECVD (Plasma Enhanced Chemical Vapor Deposition). Il y a juste le dépôt du contact Argent Ag sur la face avant de la plaquette. Nous avons utilisé la pâte de sérigraphie Ag Ferro 3349. La grille métallique comporte six (06) motifs TLM (Transfer Length Method) pour les mesures de la résistance de contact. Le principal but de ce travail est le contrôle de la qualité du contact Ag/SiNx/n+-Si dans les cellules solaires au silicium multicristallin. Les mesures TLM révèlent une cartographie des valeurs de la résistance de contact pour chaque température. Le profil optimal de température de recuit est autour de 750 °C

Reply to Comment on "Criterion that Determines the Foldability of Proteins"

We point out that the correlation between folding times and $\sigma = (T_{\theta } - T_{f})/T_{\theta }$ in protein-like heteropolymer models where $T_{\theta }$ and $T_{f}$ are the collapse and folding transition temperatures was already established in 1993 before the other presumed equivalent criterion (folding times correlating with $T_{f}$ alone) was suggested. We argue that the folding times for these models show no useful correlation with the energy gap even if restricted to the ensemble of compact structures as suggested by Karplus and Shakhnovich (cond-mat/9606037).Comment: 6 pages, Latex, 2 Postscript figures. Plots explicitly showing the lack of correlation between folding time and energy gap are adde

Optimal shapes of compact strings

Optimal geometrical arrangements, such as the stacking of atoms, are of relevance in diverse disciplines. A classic problem is the determination of the optimal arrangement of spheres in three dimensions in order to achieve the highest packing fraction; only recently has it been proved that the answer for infinite systems is a face-centred-cubic lattice. This simply stated problem has had a profound impact in many areas, ranging from the crystallization and melting of atomic systems, to optimal packing of objects and subdivision of space. Here we study an analogous problem--that of determining the optimal shapes of closely packed compact strings. This problem is a mathematical idealization of situations commonly encountered in biology, chemistry and physics, involving the optimal structure of folded polymeric chains. We find that, in cases where boundary effects are not dominant, helices with a particular pitch-radius ratio are selected. Interestingly, the same geometry is observed in helices in naturally-occurring proteins.Comment: 8 pages, 3 composite ps figure

The RCK2 domain of the human BKCa channel is a calcium sensor

Large conductance voltage and Ca2+-dependent K+ channels (BKCa) are activated by both membrane depolarization and intracellular Ca2+. Recent studies on bacterial channels have proposed that a Ca2+-induced conformational change within specialized regulators of K+ conductance (RCK) domains is responsible for channel gating. Each pore-forming α subunit of the homotetrameric BKCa channel is expected to contain two intracellular RCK domains. The first RCK domain in BKCa channels (RCK1) has been shown to contain residues critical for Ca2+ sensitivity, possibly participating in the formation of a Ca2+-binding site. The location and structure of the second RCK domain in the BKCa channel (RCK2) is still being examined, and the presence of a high-affinity Ca2+-binding site within this region is not yet established. Here, we present a structure-based alignment of the C terminus of BKCa and prokaryotic RCK domains that reveal the location of a second RCK domain in human BKCa channels (hSloRCK2). hSloRCK2 includes a high-affinity Ca2+-binding site (Ca bowl) and contains similar secondary structural elements as the bacterial RCK domains. Using CD spectroscopy, we provide evidence that hSloRCK2 undergoes a Ca2+-induced change in conformation, associated with an α-to-β structural transition. We also show that the Ca bowl is an essential element for the Ca2+-induced rearrangement of hSloRCK2. We speculate that the molecular rearrangements of RCK2 likely underlie the Ca2+-dependent gating mechanism of BKCa channels. A structural model of the heterodimeric complex of hSloRCK1 and hSloRCK2 domains is discussed

Localization transition of random copolymers at interfaces

We consider adsorption of random copolymer chains onto an interface within the model of Garel et al. Europhysics Letters 8, 9 (1989). By using the replica method the adsorption of the copolymer at the interface is mapped onto the problem of finding the ground state of a quantum mechanical Hamiltonian. To study this ground state we introduce a novel variational principle for the Green's function, which generalizes the well-known Rayleigh-Ritz method of Quantum Mechanics to nonstationary states. Minimization with an appropriate trial Green's function enables us to find the phase diagram for the localization-delocalization transition for an ideal random copolymer at the interface.Comment: 5 page

An Analytical Approach to the Protein Designability Problem

We present an analytical method for determining the designability of protein structures. We apply our method to the case of two-dimensional lattice structures, and give a systematic solution for the spectrum of any structure. Using this spectrum, the designability of a structure can be estimated. We outline a heirarchy of structures, from most to least designable, and show that this heirarchy depends on the potential that is used.Comment: 16 pages 4 figure

Modeling study on the validity of a possibly simplified representation of proteins

The folding characteristics of sequences reduced with a possibly simplified representation of five types of residues are shown to be similar to their original ones with the natural set of residues (20 types or 20 letters). The reduced sequences have a good foldability and fold to the same native structure of their optimized original ones. A large ground state gap for the native structure shows the thermodynamic stability of the reduced sequences. The general validity of such a five-letter reduction is further studied via the correlation between the reduced sequences and the original ones. As a comparison, a reduction with two letters is found not to reproduce the native structure of the original sequences due to its homopolymeric features.Comment: 6 pages with 4 figure