New applications that come from extending seismic networks into buildings

This thesis describes engineering applications that come from extending seismic networks into building structures. The proposed applications will benefit the data from the newly developed crowd-sourced seismic networks which are composed of low-cost accelerometers. An overview of the Community Seismic Network and the earthquake detection method are addressed. In the structural array components of crowd-sourced seismic networks, there may be instances in which a single seismometer is the only data source that is available from a building. A simple prismatic Timoshenko beam model with soil-structure interaction (SSI) is developed to approximate mode shapes of buildings using natural frequency ratios. A closed form solution with complete vibration modes is derived. In addition, a new method to rapidly estimate total displacement response of a building based on limited observational data, in some cases from a single seismometer, is presented. The total response of a building is modeled by the combination of the initial vibrating motion due to an upward traveling wave, and the subsequent motion as the low-frequency resonant mode response. Furthermore, the expected shaking intensities in tall buildings will be significantly different from that on the ground during earthquakes. Examples are included to estimate the characteristics of shaking that can be expected in mid-rise to high-rise buildings. Development of engineering applications (e.g., human comfort prediction and automated elevator control) for earthquake early warning system using probabilistic framework and statistical learning technique is addressed.

Physical characterization of the rack effect and hydrogen bond networks in blue copper proteins

A summary of previous research is presented that indicates that the purpose of a blue copper protein's fold and hydrogen bond network, aka, the rack effect, enforce a copper(II) geometry around the copper(I) ion in the metal site. In several blue copper proteins, the C-terminal histidine ligand becomes protonated and detaches from the copper in the reduced forms. Mutants of amicyanin from Paracoccus denitrificans were made to alter the hydrogen bond network and quantify the rack effect by pK_a shifts.

The pK_a's of mutant amicyanins have been measured by pH-dependent electrochemistry. P94F and P94A mutations loosen the Northern loop, allowing the reduced copper to adopt a relaxed conformation: the ability to relax drives the reduction potentials up. The measured potentials are 265 (wild type), 380 (P94A), and 415 (P94F) mV vs. NHE. The measured pK_a's are 7.0 (wild type), 6.3 (P94A), and 5.0 (P94F). The additional hydrogen bond to the thiolate in the mutants is indicated by a red-shift in the blue copper absorption and an increase in the parallel hyperfine splitting in the EPR spectrum. This hydrogen bond is invoked as the cause for the increased stability of the C-terminal imidazole.

Melting curves give a measure of the thermal stability of the protein. A thermodynamic intermediate with pH-dependent reversibility is revealed. Comparisons with the electrochemistry and apoamicyanin suggest that the intermediate involves the region of the protein near the metal site. This region is destabilized in the P94F mutant; coupled with the evidence that the imidazole is stabilized under the same conditions confirms an original concept of the rack effect: a high energy configuration is stabilized at a cost to the rest of the protein.