Ulrich Markel
RWTH Aachen University
17 Papers
34 Citations
Ulrich Markel is an academic researcher from RWTH Aachen University. The author has contributed to research in topics: Chemistry & Directed evolution. The author has an hindex of 5, co-authored 12 publications. Previous affiliations of Ulrich Markel include California Institute of Technology.
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Papers
Advances in ultrahigh-throughput screening for directed enzyme evolution
Ulrich Markel,Khalil D Essani,Volkan Besirlioglu,Johannes Schiffels,Wolfgang R. Streit,Ulrich Schwaneberg,Ulrich Schwaneberg +6 more
TL;DR: The importance of compartmentalization to preserve the essential link between genotype and phenotype is shed light on and how cells and biomimetic compartments can be applied to serve this function is discussed.
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Engineering and emerging applications of artificial metalloenzymes with whole cells
Malte Wittwer,Ulrich Markel,Johannes Schiffels,Jun Okuda,Daniel F. Sauer,Ulrich Schwaneberg,Ulrich Schwaneberg +6 more
- 01 Oct 2021
TL;DR: The field of artificial metalloenzymes (ArMs) is rapidly growing and ArMs are attracting increasing attention, for example, in the fields of biosensing and drug therapy.
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Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Haiyang Cui,Lobna Eltoukhy,Lingling Zhang,Ulrich Markel,Karl-Erich Jaeger,Mehdi D. Davari,Ulrich Schwaneberg +6 more
TL;DR: In this article, a smart salt bridge design strategy for simultaneously improving OS resistance and thermostability of the model enzyme, Bacillus subtilits Lipase (BSLA), was reported.
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Are Directed Evolution Approaches Efficient in Exploring Nature’s Potential to Stabilize a Lipase in Organic Cosolvents?
Ulrich Markel,Leilei Zhu,Victorine Josiane Frauenkron-Machedjou,Jing Zhao,Marco Bocola,Mehdi D. Davari,Karl-Erich Jaeger,Ulrich Schwaneberg +7 more
TL;DR: This is the first study that quantifies the capability of these diversity generation methods generally employed in directed evolution campaigns and compares them to the entire natural diversity with a single substitution.
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Engineering Chemoselectivity in Hemoprotein-Catalyzed Indole Amidation
TL;DR: Directed evolution involving mutagenesis of both the heme and reductase domains delivered an enzyme providing the desired indole amidation products with up to 8400 turnovers, 90% yield, and a shift in chemoselectivity from 2:19:1 to 110:12:1 in favor of nitrene transfer over reduction or triazole formation.
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