Detection prospects of light pseudoscalar Higgs boson at the LHC

The discovery potential of light pseudo scalar Higgs boson for the mass range 10-60 GeV is explored. In the context of the next-to-minimal supersymmetric standard(NMSSM) model, the branching fraction of light pseudo scalar Higgs boson decaying to a pair of photon can be quite large. A pair of light pseudo scalar Higgs boson produced indirectly through the standard model Higgs boson decay yields multiple photons in the final state and the corresponding production rate is restricted by ATLAS data. Discussing the impact of this constraint in the NMSSM, the detection prospects of light pseudoscalar Higgs boson in the channel consisting of at least three photons, a lepton and missing transverse energy are reported. It is observed that the possibilities of finding the pseudoscalar Higgs boson for the above mass range are promising for an integrated luminosity $\mathcal{L}=100 \text{fb}^{-1}$ with moderate significances, which can reach to more than 5$\sigma$ for higher luminosity options.Comment: 24 pages, 4 figures, updated reference

IIT teams use plant extract, heat to kill skin cancer cells

“Uptake of the nanoformulation is nearly the same by normal and cancerous cells. But the extract produces elevated levels of ROS only in cancerous cells. Right now we don’t know the precise mechanism by which higher ROS is generated inside cancer cells,” says Dr. Aravind Kumar Rengan from the Department of Biomedical Engineering at IIT Hyderabad and one of the corresponding authors of the paper. The levels of ROS inside normal cells were insignificant

Structure and sequence analyses of Bacteroides proteins BVU_4064 and BF1687 reveal presence of two novel predominantly-beta domains, predicted to be involved in lipid and cell surface interactions.

BackgroundN-terminal domains of BVU_4064 and BF1687 proteins from Bacteroides vulgatus and Bacteroides fragilis respectively are members of the Pfam family PF12985 (DUF3869). Proteins containing a domain from this family can be found in most Bacteroides species and, in large numbers, in all human gut microbiome samples. Both BVU_4064 and BF1687 proteins have a consensus lipobox motif implying they are anchored to the membrane, but their functions are otherwise unknown. The C-terminal half of BVU_4064 is assigned to protein family PF12986 (DUF3870); the equivalent part of BF1687 was unclassified.ResultsCrystal structures of both BVU_4064 and BF1687 proteins, solved at the JCSG center, show strikingly similar three-dimensional structures. The main difference between the two is that the two domains in the BVU_4064 protein are connected by a short linker, as opposed to a longer insertion made of 4 helices placed linearly along with a strand that is added to the C-terminal domain in the BF1687 protein. The N-terminal domain in both proteins, corresponding to the PF12985 (DUF3869) domain is a β-sandwich with pre-albumin-like fold, found in many proteins belonging to the Transthyretin clan of Pfam. The structures of C-terminal domains of both proteins, corresponding to the PF12986 (DUF3870) domain in BVU_4064 protein and an unclassified domain in the BF1687 protein, show significant structural similarity to bacterial pore-forming toxins. A helix in this domain is in an analogous position to a loop connecting the second and third strands in the toxin structures, where this loop is implicated to play a role in the toxin insertion into the host cell membrane. The same helix also points to the groove between the N- and C-terminal domains that are loosely held together by hydrophobic and hydrogen bond interactions. The presence of several conserved residues in this region together with these structural determinants could make it a functionally important region in these proteins.ConclusionsStructural analysis of BVU_4064 and BF1687 points to possible roles in mediating multiple interactions on the cell-surface/extracellular matrix. In particular the N-terminal domain could be involved in adhesive interactions, the C-terminal domain and the inter-domain groove in lipid or carbohydrate interactions