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Lining Mao

Publications and source records attributed to Lining Mao.

2 recordsLinked to original sources

Comprehensive reconstruction of collider events with hypergraph representation learning and graph-conditioned diffusion

In particle collider experiments, event reconstruction is the task of inferring the kinematics of short-lived particles produced in the hard scatter from the stable final states recorded by detectors. We decompose event reconstruction into two primary tasks: assigning measured jets and charged leptons to parent particles, and predicting unmeasured neutrino kinematics. We present VyPER, a novel geometric learning framework that represents collider events as hypergraphs with a physics-inspired topology. VyPER combines the supervised classification of hyperedges for particle assignment with a diffusion model for predicting neutrino kinematics, leveraging a joint loss function to optimize both reconstruction tasks within a unified framework. We showcase VyPER across several proton-proton collision processes, comparing its performance to existing analytical and machine-learning-based reconstruction techniques. In doing so, we demonstrate that accurate event reconstruction is achievable across a diverse range of Standard Model physics processes, opening new avenues for precision measurements in the Higgs boson, electroweak, and top-quark sectors.

hep-ph

ProTDyn: a foundation Protein language model for Thermodynamics and Dynamics generation

Molecular dynamics (MD) simulation has long been the principal computational tool for exploring protein conformational landscapes and dynamics, but its application is limited by high computational cost. We present ProTDyn, a foundation protein language model that unifies conformational ensemble generation and multi-timescale dynamics modeling within a single framework. Unlike prior approaches that treat these tasks separately, ProTDyn allows flexible independent and identically distributed (i.i.d.) ensemble sampling and dynamic trajectory simulation. Across diverse protein systems, ProTDyn yields thermodynamically consistent ensembles, faithfully reproduces dynamical properties over multiple timescales, and generalizes to proteins beyond its training data. It offers a scalable and efficient alternative to conventional MD simulations.

physics.bio-ph