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A covalently bound catalytic intermediate in Escherichia coli asparaginase : Crystal structure of a Thr‐89‐Val mutant
Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis, and the previously identified oxyanion hole is described in more detail.
Dynamics of a mobile loop at the active site of Escherichia coli asparaginase.
Numerical simulations of the observed transients are consistent with a model where loop closure is an absolute prerequisite for substrate turnover, and indicates that the presence of tyrosine in position 25 is essential for both loop closure and catalysis.
Multi-attribute PAT for UF/DF of Proteins—Monitoring Concentration, particle sizes, and Buffer Exchange
The developed setup provides a powerful testing system for evaluating different UF/DF processes and may be a good starting point to develop process control strategies.