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Center for Nonlinear Studies |
A detailed knowledge of the processes by that proteins fold, change their structure and function, or self-assemble and aggregate, is crucial for an understanding of disease pathways and the working of drugs at the level of cells. As these fundamental processes are difficult to trace, there is a need for reliable computational tools that can complement experiments. In this talk, I will describe some of the methods that are transforming computer simulations into virtual microscopes. These techniques will be discussed in the context of folding and conversion of certain proteins which switch their structure according to the desired function. In the second half I will focus on the formation and propagation of protein aggregates that are associated with various diseases.
Selected Publications:N.A. Bernhardt, W. Xi, W. Wang and U.H.E. Hansmann, Simulating Protein Fold Switching by Replica-Exchange-with-Tunneling, J. Chem. Theor. Comp. 12 (2016)5656.
W. Xi and U.H.E. Hansmann, Ring-like N-fold Models of Aβ42 fibrils, Scientific Report,7 (2017) 6588.
W. Xi and U.H.E. Hansmann, Conversion between parallel and antiparallel β-sheetsin wild type and Iowa mutant Aβ40 fibrils, J. Chem. Phys., 148 (2018) 045103.
W. Xi, D.N. Dean, K.A. Stockmal, S.E. Morgan, U.H.E. Hansmann and V.Rangachari, Large Fatty Acid-derived Aβ42 oligomers Form Ring-like Assemblies, J.Chem. Phys. 150 (2019) 075101.
Host: Christoph Junghans