Density functional calculations of the electronic structure and magnetic properties of the hydrocarbon K3picene superconductor near the metal-insulator transition

We have investigated the electronic structures and magnetic properties of of K3picene, which is a first hydrocarbon superconductor with high transition temperature T_c=18K. We have shown that the metal-insulator transition (MIT) is driven in K3picene by 5% volume enhancement with a formation of local magnetic moment. Active bands for superconductivity near the Fermi level E_F are found to have hybridized character of LUMO and LUMO+1 picene molecular orbitals. Fermi surfaces of K3picene manifest neither prominent nesting feature nor marked two-dimensional behavior. By estimating the ratio of the Coulomb interaction U and the band width W of the active bands near E_F, U/W, we have demonstrated that K3picene is located in the vicinity of the Mott transition.Comment: 5 pages, 5 figure

Two-gap and paramagnetic pair-breaking effects on upper critical field of SmFeAsO0.85_{0.85} and SmFeAsO0.8_{0.8}F0.2_{0.2} single crystals

We investigated the temperature dependence of the upper critical field [$H_{c2}(T)$] of fluorine-free SmFeAsO$_{0.85}$ and fluorine-doped SmFeAsO$_{0.8}$F$_{0.2}$ single crystals by measuring the resistive transition in low static magnetic fields and in pulsed fields up to 60 T. Both crystals show that $H_{c2}(T)$'s along the c axis [$H_{c2}^c(T)$] and in an $ab$-planar direction [$H_{c2}^{ab}(T)$] exhibit a linear and a sublinear increase, respectively, with decreasing temperature below the superconducting transition. $H_{c2}(T)$'s in both directions deviate from the conventional one-gap Werthamer-Helfand-Hohenberg theoretical prediction at low temperatures. A two-gap nature and the paramagnetic pair-breaking effect are shown to be responsible for the temperature-dependent behavior of $H_{c2}^c$ and $H_{c2}^{ab}$, respectively.Comment: 21 pages, 8 figure

A mechanism for robust circadian timekeeping via stoichiometric balance

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/102189/1/msb201262.reviewer_comments.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/102189/2/msb201262.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/102189/3/msb201262-sup-0001.pd

Proteomic analysis of Bifidobacterium longum subsp. infantis reveals the metabolic insight on consumption of prebiotics and host glycans.

Bifidobacterium longum subsp. infantis is a common member of the intestinal microbiota in breast-fed infants and capable of metabolizing human milk oligosaccharides (HMO). To investigate the bacterial response to different prebiotics, we analyzed both cell wall associated and whole cell proteins in B. infantis. Proteins were identified by LC-MS/MS followed by comparative proteomics to deduce the protein localization within the cell. Enzymes involved in the metabolism of lactose, glucose, galactooligosaccharides, fructooligosaccharides and HMO were constitutively expressed exhibiting less than two-fold change regardless of the sugar used. In contrast, enzymes in N-Acetylglucosamine and sucrose catabolism were induced by HMO and fructans, respectively. Galactose-metabolizing enzymes phosphoglucomutase, UDP-glucose 4-epimerase and UTP glucose-1-P uridylytransferase were expressed constitutively, while galactokinase and galactose-1-phosphate uridylyltransferase, increased their expression three fold when HMO and lactose were used as substrates for cell growth. Cell wall-associated proteomics also revealed ATP-dependent sugar transport systems associated with consumption of different prebiotics. In addition, the expression of 16 glycosyl hydrolases revealed the complete metabolic route for each substrate. Mucin, which possesses O-glycans that are structurally similar to HMO did not induced the expression of transport proteins, hydrolysis or sugar metabolic pathway indicating B. infantis do not utilize these glycoconjugates