Jet cross sections at the LHC and the quest for higher precision.

We perform a phenomenological study of Z plus jet, Higgs plus jet and di-jet production at the Large Hadron Collider. We investigate in particular the dependence of the leading jet cross section on the jet radius as a function of the jet transverse momentum. Theoretical predictions are obtained using perturbative QCD calculations at the next-to and next-to-next-to-leading order, using a range of renormalization and factorization scales. The fixed order predictions are compared to results obtained from matching next-to-leading order calculations to parton showers. A study of the scale dependence as a function of the jet radius is used to provide a better estimate of the scale uncertainty for small jet sizes. The non-perturbative corrections as a function of jet radius are estimated from different generators.

Beyond standard model calculations with Sherpa.

We present a fully automated framework as part of the Sherpa event generator for the computation of tree-level cross sections in Beyond Standard Model scenarios, making use of model information given in the Universal FeynRules Output format. Elementary vertices are implemented into C++ code automatically and provided to the matrix-element generator Comix at runtime. Widths and branching ratios for unstable particles are computed from the same building blocks. The corresponding decays are simulated with spin correlations. Parton showers, QED radiation and hadronization are added by Sherpa, providing a full simulation of arbitrary BSM processes at the hadron level.

Assisted peptide folding by surface pattern recognition.

Natively disordered proteins belong to a unique class of biomolecules whose function is related to their flexibility and their ability to adopt desired conformations upon binding to substrates. In some cases these proteins can bind multiple partners, which can lead to distinct structures and promiscuity in functions. In other words, the capacity to recognize molecular patterns on the substrate is often essential for the folding and function of intrinsically disordered proteins. Biomolecular pattern recognition is extremely relevant both in vivo (e.g., for oligomerization, immune response, induced folding, substrate binding, and molecular switches) and in vitro (e.g., for biosensing, catalysis, chromatography, and implantation). Here, we use a minimalist computational model system to investigate how polar/nonpolar patterns on a surface can induce the folding of an otherwise unstructured peptide. We show that a model peptide that exists in the bulk as a molten globular state consisting of many interconverting structures can fold into either a helix-coil-helix or an extended helix structure in the presence of a complementary designed patterned surface at low hydrophobicity (3.7%) or a uniform surface at high hydrophobicity (50%). However, we find that a carefully chosen surface pattern can bind to and catalyze the folding of a natively unfolded protein much more readily or effectively than a surface with a noncomplementary or uniform distribution of hydrophobic residues.