Cyclotron resonance in HgTe/CdTe-based heterostructures in high magnetic fields

Cyclotron resonance study of HgTe/CdTe-based quantum wells with both inverted and normal band structures in quantizing magnetic fields was performed. In semimetallic HgTe quantum wells with inverted band structure, a hole cyclotron resonance line was observed for the first time. In the samples with normal band structure, interband transitions were observed with wide line width due to quantum well width fluctuations. In all samples, impurity-related magnetoabsorption lines were revealed. The obtained results were interpreted within the Kane 8·8 model, the valence band offset of CdTe and HgTe, and the Kane parameter E(P) being adjusted

Modeling protein network evolution under genome duplication and domain shuffling

<p>Abstract</p> <p>Background</p> <p>Successive whole genome duplications have recently been firmly established in all major eukaryote kingdoms. Such <it>exponential </it>evolutionary processes must have largely contributed to shape the topology of protein-protein interaction (PPI) networks by outweighing, in particular, all <it>time-linear </it>network growths modeled so far.</p> <p>Results</p> <p>We propose and solve a mathematical model of PPI network evolution under successive genome duplications. This demonstrates, from first principles, that evolutionary conservation and scale-free topology are intrinsically linked properties of PPI networks and emerge from <it>i) </it>prevailing <it>exponential </it>network dynamics under duplication and <it>ii) asymmetric divergence </it>of gene duplicates. While required, we argue that this asymmetric divergence arises, in fact, spontaneously at the level of protein-binding sites. This supports a refined model of PPI network evolution in terms of protein domains under exponential and asymmetric duplication/divergence dynamics, with multidomain proteins underlying the combinatorial formation of protein complexes. Genome duplication then provides a powerful source of PPI network innovation by promoting local rearrangements of multidomain proteins on a genome wide scale. Yet, we show that the overall conservation and topology of PPI networks are robust to extensive domain shuffling of multidomain proteins as well as to finer details of protein interaction and evolution. Finally, large scale features of <it>direct </it>and <it>indirect </it>PPI networks of <it>S. cerevisiae </it>are well reproduced numerically with only two adjusted parameters of clear biological significance (<it>i.e</it>. network effective growth rate and average number of protein-binding domains per protein).</p> <p>Conclusion</p> <p>This study demonstrates the statistical consequences of genome duplication and domain shuffling on the conservation and topology of PPI networks over a broad evolutionary scale across eukaryote kingdoms. In particular, scale-free topologies of PPI networks, which are found to be robust to extensive shuffling of protein domains, appear to be a simple consequence of the conservation of protein-binding domains under asymmetric duplication/divergence dynamics in the course of evolution.</p

Additional file 6: Figure S2. of Cross-disorder comparative analysis of comorbid conditions reveals novel autism candidate genes

First two Multidimensional Scaling (MDS) dimensions of our dataset generated by MDS on a dissimilarity matrix using Jaccard Coefficient when k = 6. Each group is highlighted in a different color and the disorders conforming them are detailed in Additional file 5: Table S4, along with their corresponding mean Jaccard Coefficient value. The autism sibling comorbid disorders are clustered together in group 2 (PDF 180 kb