Development of a didactic demonstrator for flow-induced noise mechanisms and mitigation technologies.

A small didactic wind tunnel demonstrator has been designed and manufactured at the von Karman Institute for Fluid Dynamics to illustrate the physical principles at stake in flow-induced noise generation, offer an audible perception of the effectiveness of noise-mitigation strategies, and serve as a practical test bench for aeroacoustic education and research. Seven mitigation technologies are embedded in a single facility, which addresses the noise generation by an airfoil, noise propagation in a duct, and noise transmission through a flexible panel. A challenging objective of this facility was to offer a perceptible impression of various aeroacoustic noise mechanisms at low flow speeds and a live assessment of the effectiveness of noise-reduction technologies. Different approaches combining multiple microphones, advanced signal-processing techniques, and real-time audio feedback have been implemented to this end. A digital twin has been developed to assist the design of the facility and test the concepts implemented in it. The results establish that the demonstrator enables a clear perception of the effectiveness of the noise-mitigation technologies. The facility is also suitable for fast and inexpensive preliminary investigations of future noise-reduction concepts, taking advantage of rapid prototyping techniques.

A repertoire library that allows the selection of synthetic SH2s with altered binding specificities.

Tyrosine phosphorylation is one of the major mechanisms involved in the intracellular propagation of external signals. Strategies aimed at interfering with this process might allow the control of several cellular phenotypes. SH2 domains mediate protein-protein interactions by recognizing phosphotyrosine (pY) residues in the context of specific phosphopeptides. We created an SH2-scaffolded repertoire library by randomly mutagenizing five critical amino acid positions in the specificity-determining region of the PLCgamma C-terminal SH2 domain. Synthetic SH2 domains were selected from the library using biotinylated phosphopeptides derived from a natural PLCgamma-SH2 ligand as well as unrelated SH2 ligands. The isolated SH2s displayed high binding affinity constants for the selecting peptides and were capable of interacting with the corresponding proteins.