Dr Daniel Dunkelmann is Nevile Research Fellow at Magdalene.
As a synthetic biologist, Daniel focuses on equipping biological systems with chemical tools to unlock the power of cells as factories with highly tuned molecular machines, which precisely assemble artificial materials.
In his PhD with Prof. Jason Chin at the MRC Laboratory of Molecular Biology, he has discovered and engineered molecular machines and developed methodologies, which enable the facile incorporation of multiple artificial building blocks into proteins. As a Junior Research Fellow at Magdalene College, he will focus on fundamentally changing the nature of the building blocks that the cellular protein production machinery can assemble.
Daniel studied interdisciplinary sciences at the Federal Institute of Technology (ETH) in Zurich, where he graduated with a Bsc and Msc degree. As an Erasmus fellow he conducted research for his bachelor thesis in organic chemistry with Prof. Alan Spivey at Imperial College London. He then moved to Boston as a visiting researcher at the Massachusetts Institute of Technology (MIT), developing a peptide ligation method with Prof. Bradley Pentelute. He got introduced to the field of genetic code expansion during his master thesis in the laboratory of Prof. Don Hilvert at ETH. Before starting his PhD in synthetic biology he joined the laboratory of Prof. Hiroaki Suga at the University of Tokyo as an ETH worldwide fellow.
PhD in Biological Sciences, MRC Laboratory of Molecular Biology, University of Cambridge, UK.
MSc in Interdisciplinary Science, ETH Zurich, Switzerland
BSc in Interdisciplinary Science, ETH Zurich, Switzerland
Total synthesis of Escherichia coli with a recoded genome
Dunkelmann DL, Oehm SB, Beattie AT and Chin JW Nature Chemistry 2021, 13, 1110–1117
Engineered triply orthogonal pyrrolysyl–tRNA synthetase/tRNA pairs enable the genetic encoding of three distinct non-canonical amino acids
Dunkelmann DL, Willis JW, Beattie AT and Chin JW Nature Chemistry 2020, 12, 535-544
Amide-forming chemical ligation via O-acyl hydroxamic acids
Dunkelmann DL, Hirata Y, Totaro KA, Cohen DT, Zhang C, Gates ZP and Pentelute BL Proceedings of the National Academy of Sciences of the United States2018, 114 (15), 3752-3757