In this study we investigated the capabilities of the mesh-free, Lagrangian particle method (Smoothed Particle Hydrodynamics, SPH) to simulate the detailed hydrodynamic processes generated by both spilling and plunging breaking waves within the surf zone. The weakly-compressible SPH code DualSPHysics was applied to simulate wave breaking over two distinct bathymetric profiles (a plane beach and fringing reef) and compared to experimental flume measurements of waves, flows, and mean water levels. Despite the simulations spanning very different wave breaking conditions (including an extreme case with violently plunging waves on an effectively dry reef slope), the model was able to reproduce a wide range of relevant surf zone hydrodynamic processes using a fixed set of numerical parameters. This included accurate predictions of the nonlinear evolution of wave shapes (e.g., asymmetry and skewness properties), rates of wave dissipation within the surf zone, and wave setup distributions. By using this mesh-free approach, the model was able to resolve the critical crest region within the breaking waves, which provided robust predictions of the wave-induced mass fluxes within the surf zone responsible for the undertow. Within this breaking crest region, the model results capture how the potential energy of the organized wave motion is initially converted to kinetic energy and then dissipated, which reproduces the distribution of wave forces responsible for wave setup generation across the surf zone. Overall, the results reveal how the mesh-free SPH approach can accurately reproduce the detailed wave breaking processes with comparable skill to state-of-the-art mesh-based Computational Fluid Dynamics (CFD) models, and thus can be applied to provide valuable new physical insight into surf zone dynamics.@en

Proteins are vital in all biological systems as they constitute the main structural and functional components of cells. Recent advances in mass spectrometry have brought the promise of complete proteomics by helping draft the human proteome. Yet, this commonly used protein sequencing technique has fundamental limitations in sensitivity. Here we propose a method for single-molecule (SM) protein sequencing. A major challenge lies in the fact that proteins are composed of 20 different amino acids, which demands 20 molecular reporters. We computationally demonstrate that it suffices to measure only two types of amino acids to identify proteins and suggest an experimental scheme using SM fluorescence. When achieved, this highly sensitive approach will result in a paradigm shift in proteomics, with major impact in the biological and medical sciences.@en