Search results for: Kim A. Timm

Authors: Yashved Serhun, Kim A. Timm

Abstract:

Barclays Bank has identified the need for a head office building in Lusaka, Zambia, and construction of a 7200 m2 three-storey reinforced concrete office building with a structural steel roof is currently underway. A unique characteristic of the development is that the building footprint is positioned on dolomitic land. Dolomite rock has the tendency to react with and breakdown in the presence of slightly acidic water, including rainwater. This leads to a potential for subsidence and sinkhole formation. Subsidence and the formation of sinkholes beneath a building can be detrimental during both the construction and operational phases. This paper outlines engineering principles which were considered during the structural design of the raft foundation for the Barclays head office building. In addition, this paper includes multidisciplinary considerations and the impact of these on the structural engineering design of the raft foundation. By ensuring that the design of raft foundations on dolomitic land incorporates the requirements of all disciplines and relevant design codes during the design process, the risk associated with subsidence and sinkhole formation can be effectively mitigated during the operational phase of the building.

Keywords: dolomite, dolomitic land, raft foundation, structural engineering design

Procedia PDF Downloads 96

Authors: Saroj Poudel, Joshua Mancini, Douglas Pike, Jennifer Timm, Alexei Tyryshkin, Vikas Nanda, Paul Falkowski

Abstract:

On the early Earth, protein-metal complexes likely harvested energy from a reduced environment. These complexes would have been precursors to the metabolic enzymes of ancient organisms. Hydrogenase is an essential enzyme in most anaerobic organisms for the reduction and oxidation of hydrogen in the environment and is likely one of the earliest evolved enzymes. To attempt to reinvent a precursor to modern hydrogenase, we computationally designed a short thirteen amino acid peptide that binds the often-required catalytic transition metal Nickel in hydrogenase. This simple complex can achieve hundreds of hydrogen evolution cycles using light energy in a broad range of temperature and pH. Biophysical and structural investigations strongly indicate the peptide forms a di-nickel active site analogous to Acetyl-CoA synthase, an ancient protein central to carbon reduction in the Wood-Ljungdahl pathway and capable of hydrogen evolution. This work demonstrates that prior to the complex evolution of multidomain enzymes, early peptide-metal complexes could have catalyzed energy transfer from the environment on the early Earth and enabled the evolution of modern metabolism

Keywords: hydrogenase, prebiotic enzyme, metalloenzyme, computational design

Procedia PDF Downloads 192