Building structure-borne noise measurements and estimation due to train operations in tunnel.

The perception of structure-borne noise is particularly salient when train passes through the tunnel under the buildings, which has a negative impact on human health. In the process of constructing buildings along metro lines, it is crucial to estimate indoor structure-borne noise levels in order to enhance design and prevent any negative impact on human comfort. This study conducted measurements of structure-borne noise, reverberation time, and train-induced vibrations in Guangzhou, China to investigate the generation, propagation, and dissipation mechanisms of structure-borne noise. An approach based on Short-Time Fourier Transform and Schroeder integral was proposed for obtaining frequency-dependent reverberation time. Additionally, a deep learning-based approach incorporating indoor vibrations, frequency-dependent reverberation time, and room parameters as inputs was proposed based on Genetic Algorithm-Artificial Neural Network. The estimated structure-borne noise levels demonstrated good agreement with measured values, indicating the feasibility of the approach. The finding of this research facilitates a clear comprehension of the generation, distribution, and dissipation mechanisms of indoor structure-borne noise for engineers while also enabling convenient acquisition of indoor structure-borne noise. The estimated noise levels can be effectively utilized during building design processes along metro lines to mitigate adverse impacts on human comfort.

The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies.

Dimerization of the transmembrane (TM) adaptor protein DAP12 plays a key role in mediating activation signals through TM-TM association with cell-surface receptors. Herein, we apply the TOXCAT assay and molecular dynamics simulation to analyze dynamics and dimerization of the TM helix of DAP12 in the membrane bilayer. In the TOXCAT assay, we performed site-specific mutagenesis of potential dimerization motifs in the DAP12 TM domain. Instead of the common GxxxG dimerization motif, mutating either of the polar residues Asp-50 and Thr-54 significantly decreased the TOXCAT signal for the dimerization of DAP12 TM domain. Furthermore, through the conformational difference between wild-type and mutant DAP12 TM homodimers, a combined coarse-grained and atomistic molecular dynamics simulation has identified both Asp-50 and Thr-54 at the dimerization interface. The experimental and computational results of the DAP12 TM dimer are in excellent agreement with the previously reported NMR structure obtained in detergent micelles. Such a combination of dynamics simulation and cell-based experiments can be applied to produce insights at the molecular level into the TM-TM association of many other transmembrane proteins.