Isolating a light Higgs boson from the di-photon background at the LHC

We compute the QCD corrections to the gluon fusion subprocess gg to gamma gamma, which forms an important component of the background to the search for a light Higgs boson at the LHC. We study the dependence of the improved pp to gamma gamma X background calculation on the factorization and renormalization scales, on various choices for photon isolation cuts, and on the rapidities of the photons. We also investigate ways to enhance the statistical significance of the Higgs signal in the di-photon channel.Comment: Additional reference included, 17 pages, 16 figure files, revte

Two-Loop Helicity Amplitudes for Quark-Gluon Scattering in QCD and Gluino-Gluon Scattering in Supersymmetric Yang-Mills Theory

We present the two-loop QCD helicity amplitudes for quark-gluon scattering, and for quark-antiquark annihilation into two gluons. These amplitudes are relevant for next-to-next-to-leading order corrections to (polarized) jet production at hadron colliders. We give the results in the `t Hooft-Veltman and four-dimensional helicity (FDH) variants of dimensional regularization. The transition rules for converting the amplitudes between the different variants are much more intricate than for the previously discussed case of gluon-gluon scattering. Summing our two-loop expressions over helicities and colors, and converting to conventional dimensional regularization, gives results in complete agreement with those of Anastasiou, Glover, Oleari and Tejeda-Yeomans. We describe the amplitudes for 2 to 2 scattering in pure N=1 supersymmetric Yang-Mills theory, obtained from the QCD amplitudes by modifying the color representation and multiplicities, and verify supersymmetry Ward identities in the FDH scheme.Comment: 77 pages. v2: corrected errors in eqs. (3.7) and (3.8) for one-loop assembly; remaining results unaffecte

Molecular evolution of peptide tyrosine–tyrosine: primary structure of PYY from the lampreys Geotria australis and Lampetra fluviatilis, bichir, python and desert tortoise

Peptide tyrosine–tyrosine (PYY) has been isolated from the intestines of two species of reptile, the desert tortoise Gopherus agassizii (Testudines) and the Burmese python Python molurus (Squamata), from the primitive Actinopterygian fish, the bichir Polypterus senegalis (Polypteriformes) and from two agnathans, the Southern-hemisphere lamprey Geotria australis (Geotriidae) and the holarctic lamprey Lampetra fluviatilis (Petromyzontidae). The primary structure of bichir PYY is identical to the proposed ancestral sequence of gnathostome PYY (YPPKPENPGE10 | DAPPEELAKY20 | YSALR HYINL30 | ITRQRY). Tortoise and python PYY differ by six and seven residues, respectively, from the ancestral sequence consistent with the traditional view that the Testudines represent an earlier divergence from the primitive reptilian stock than the Squamates. The current views of agnathan phylogeny favor the hypothesis that the Southern-hemisphere lampreys and the holarctic lampreys arose from a common ancestral stock but their divergence is of a relatively ancient (pre-Tertiary) origin. The Geotria PYY-related peptide shows only two amino acid substitutions (Pro10→Gln and Leu22→Ser) compared with PYY from the holarctic lamprey Petromyzon marinus. This result was unexpected as Petromyzon PYY differs from Lampetra PYY deduced from the nucleotide sequence of a cDNA (Söderberg et al. J. Neurosci. Res. 1994;37:633–640) by 10 residues. However, a re-examination of an extract of Lampetra intestine revealed the presence of a PYY that differed in primary structure from Petromyzon PYY by only one amino acid residue (Pro10→Ser). This result suggests that the structure of PYY has been strongly conserved during the evolution of Agnatha and that at least two genes encoding PYY-related peptides are expressed in Lampetra tissues

Characterization of Bradykinin-related peptides generated in the plasma of six Sarcopterygian species (African lungfish, Amphiuma, Coachwhip, Bullsnake, Gila monster, and Gray's monitor)

Incubation of heat-denatured plasma from six species occupying different evolutionary positions within the Sarcopterygian lineage [the dipnoan, Protopterus annectens (African lungfish); the urodele, Amphiuma tridactylum (three-toed amphiuma); the colubrid snakes, Pituophis melanoleucus sayi (bullsnake) and Masticophis flagellum (coachwhip); and the lizards Heloderma suspectum (Gila monster) and Varanus Grayi (Gray's monitor)] with trypsin generated bradykinin-related peptides that were detected by radioimmunoassay using an antiserum raised against mammalian bradykinin (BK). The peptides were purified by HPLC and their primary structures were established as lungfish [Tyr1,Gly2,Ala7,Pro8]BK, amphiuma [Phe1,Ile2, Leu5]BK, bullsnake and coachwhip [Val1,Thr6]BK, Gila monster [Leu2, Thr6]BK, and Gray's monitor [Thr6]BK. Monitor BK is identical to the peptide generated in turtle and alligator plasma and coachwhip/bullsnake BK shows one amino acid substitution (Ala1 --> Val) compared with the peptide generated in the plasma of the python. The data provide further evidence for the widespread occurrence of a kallikrein-kininogen system in nonmammalian vertebrates but indicate that the primary structure of BK has been poorly conserved during evolution