Field and laboratory experiments were performed to unravel the structure of the power output fluctuations of horizontal-axis wind turbines based on incoming flow turbulence. The study considers the power data of three wind turbines of rotor sizes 0.12, 3.2, and 96 m, with rated power spanning six decades from the order of 10 0 to 10 6 W. The 0.12 m wind turbine was tested in a wind tunnel while the 3.2 and 96 m wind turbines were operated in open fields under approximately neutrally stratified thermal conditions. Incoming flow turbulence was characterised by hotwire and sonic anemometers for the wind tunnel and field set-ups. While previous works have observed a filtering behaviour in wind turbine power output, this exact behaviour has not, to date, been properly characterised. Based on the spectral structure of the incoming flow turbulence at hub height, and the mechanical and structural properties of the turbines, a physical basis for the behaviour of temporal power fluctuations and their spectral structure is found with potential applications in turbine control and numerical simulations. Consistent results are observed across the geometrical scales of the wind turbines investigated, suggesting no Reynolds number dependence in the tested range.

Surface-enhanced Raman spectroscopy (SERS) has emerged as a powerful tool to detect biomolecules in aqueous environments. However, it is challenging to identify protein structures at low concentrations, especially for the proteins existing in an equilibrium mixture of various conformations. Here, we develop an in situ optical tweezers-coupled Raman spectroscopy to visualize and control the hotspot between two Ag nanoparticle-coated silica beads, generating tunable and reproducible SERS enhancements with single-molecule level sensitivity. This dynamic SERS detection window is placed in a microfluidic flow chamber to detect the passing-by proteins, which precisely characterizes the structures of three globular proteins without perturbation to their native states. Moreover, it directly identifies the structural features of the transient species of alpha-synuclein among its predominant monomers at physiological concentration of 1 μM by reducing the ensemble averaging. Hence, this SERS platform holds the promise to resolve the structural details of dynamic, heterogeneous, and complex biological systems.

A series of new homopolymers with various degrees of polymerization derived from vinyl tetraphenylethene, that is, poly[2-(4-vinylphenyl)ethene-1,1,2-triyl)tribenzene] homopolymers, is synthesized by reversible addition-fragmentation chain transfer (RAFT) polymerization. The homopolymers exhibit a significant aggregation-induced emission (AIE) effect and an ability to assemble themselves into AIE polymer nanoparticles (NPs) during precipitation in a water/tetrahydrofuran (THF) mixture. The NPs also exhibit good dispersibility, stability, and biocompatibility. The AIE polymer NPs are used in imaging studies of HeLa cells.

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