Jason W. Chin

MRC Laboratory of Molecular Biology

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Thomas Elliott

Medical Research Council

Nicolas Huguenin‐Dezot

MRC Laboratory of Molecular Biology

Kaihang Wang

Xiamen University

Chayasith Uttamapinant

Vidyasirimedhi Institute of Science and Technology

Kathrin Lang

Technical University of Munich

Lloyd Davis

University of Edinburgh

Duy Nguyen

Heidelberg University

Wolfgang H. Schmied

Medical Research Council

Alexander Deiters

University of Pittsburgh

Peter G. Schultz

Scripps Research Institute

Cooperative Institutions

Medical Research Council

163

MRC Laboratory of Molecular Biology

157

University of Cambridge

University of Oxford

Harvard University

Howard Hughes Medical Institute

University of California, San Diego

University of California, Berkeley

University College London

University of Dundee

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Concerted, Rapid, Quantitative, and Site-Specific Dual Labeling of Proteins

Journal of the American Chemical Society (2014)

Amit Sachdeva Kaihang Wang Thomas Elliott Jason W. Chin

Rapid, one-pot, concerted, site-specific labeling of proteins at genetically encoded unnatural amino acids with distinct small molecules at physiological pH, temperature, and pressure is an important challenge. Current approaches require sequential labeling, low pH, and typically days to reach completion, limiting their utility. We report the efficient, genetically encoded incorporation of alkyne- and cyclopropene-containing amino acids at distinct sites in a protein using an optimized orthogonal translation system in E. coli. and quantitative, site-specific, one-pot, concerted protein labeling with fluorophores bearing azide and tetrazine groups, respectively. Protein double labeling in aqueous buffer at physiological pH, temperature, and pressure is quantitative in 30 min.

Tetrazine

Alkyne

Limiting

Bioorthogonal Chemistry

10.1021/ja4129789

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Citations (145)

Frontispiz: Efficient Phage Display with Multiple Distinct Non‐Canonical Amino Acids Using Orthogonal Ribosome‐Mediated Genetic Code Expansion

Angewandte Chemie (2019)

Benjamí Oller‐Salvia Jason W. Chin

Phagen-Display Die effiziente Einführung nichtkanonischer Aminosäuren in Phagen-Display-Proteine wird von J. W. Chin und B. Oller-Salvia in der Zuschrift auf S. 10960 beschrieben.

Genetic Code

Non canonical

10.1002/ange.201983261

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Desymmetrization of Meso Anhydrides

Synfacts (2008)

Stephen J. Connon Jason W. Chin Chang Eun Song

Desymmetrizations of meso anhydrides catalyzed by a cinchona alkaloid bearing a thiourea moiety are reported. Bifunctional catalyst 1 mediates the methanolysis of succinic and glutaric anhydrides 2 to give hemiesters 3 in good yields and enantioselectivities. The reactions are carried out in coordinating solvents at unusually low concentrations to prevent the dimerization or aggregation of catalyst 1 through hydrogen bonding. Its monomeric form is presumably responsible for high enantioselectivities.

Desymmetrization

Cinchona

Moiety

10.1055/s-2008-1072681

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Genetically programmed cell-based synthesis of non-natural peptide and depsipeptide macrocycles

Nature Chemistry (2022)

Martin Spinck Carlos Piedrafita Wesley E. Robertson Thomas Elliott Daniele Cervettini

The direct genetically encoded cell-based synthesis of non-natural peptide and depsipeptide macrocycles is an outstanding challenge. Here we programme the encoded synthesis of 25 diverse non-natural macrocyclic peptides, each containing two non-canonical amino acids, in Syn61Δ3-derived cells; these cells contain a synthetic Escherichia coli genome in which the annotated occurrences of two sense codons and a stop codon, and the cognate transfer RNAs (tRNAs) and release factor that normally decode these codons, have been removed. We further demonstrate that pyrrolysyl-tRNA synthetase/tRNA pairs from distinct classes can be engineered to direct the co-translational incorporation of diverse alpha hydroxy acids, with both aliphatic and aromatic side chains. We define 49 engineered mutually orthogonal pairs that recognize distinct non-canonical amino acids or alpha hydroxy acids and decode distinct codons. Finally, we combine our advances to programme Syn61Δ3-derived cells for the encoded synthesis of 12 diverse non-natural depsipeptide macrocycles, which contain two non-canonical side chains and either one or two ester bonds.

Depsipeptide

Stop codon

Peptide Synthesis

10.1038/s41557-022-01082-0

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Citations (43)

Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs

Nature Chemistry (2018)

Julian C. W. Willis Jason W. Chin

Amino Acyl-tRNA Synthetases

Genetic Code

Amino Acyl-tRNA Synthetases

10.1038/s41557-018-0052-5

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Citations (162)

DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

Nature (2012)

Simon J. Elsässer Hongda Huang Peter W. Lewis Jason W. Chin C. David Allis

Death-associated protein 6

Histone code

Histone octamer

Histone H4

10.1038/nature11608

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Citations (235)

A dual role of H4K16 acetylation in the establishment of yeast silent chromatin

The EMBO Journal (2011)

Mariano Oppikofer Stephanie Kueng Fabrizio Martino Szabolcs Soeroes Susan M. Hancock

Epigenesis

10.1038/emboj.2011.170

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Citations (94)

Labeling and identifying cell-specific proteomes in the mouse brain

Nature Biotechnology (2017)

Toke P. Krogager Russell J. Ernst Thomas Elliott Laura Calò Václav Beránek

Proteome

Cell type

Identification

10.1038/nbt.4056

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Citations (82)

Plasmodium 3D7 Genome Assembly With PacBio Data and CLEAR

Figshare (2013)

Jason W. Chin

This fileset contains data, code and IPython Notebooks demostrating
how to assemble the hard to assemble 80% AT-rich Plasmodium 3D7 genome. The first thing you might want to do is probably to read through
''P3D7_CLEAR_NOTE.pdf'' to know what this dataset is about. You will have to "gunzip" the two main data file ''preads.fa.gz'' and
''pr_pr_strigent.m4.gz'' to use them. The IPython Notebook ''P3D7_CLEAR_NOTE.ipynb'' and ''P3D7_CLEAR_NOTE_P2.ipynb''
can be run to generate the assembly if you have proper computation environment. There are also the PDF verison of the notebooks, ''P3D7_CLEAR_NOTE.pdf''
and ''P3D7_CLEAR_NOTE_P2.pdf''. Some requirement on how to reproduce the
computational experiment can be found in ''P3D7_CLEAR_NOTE.pdf''.

Sequence assembly

Plasmodium (life cycle)

10.6084/m9.figshare.712587.v4

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Design and Evolution of a Miniature Bcl-2 Binding Protein

Angewandte Chemie (2001)

Jason W. Chin Alanna Schepartz

Eine große Herausforderung für die chemische Biologie ist die Entwicklung wirksamer und selektiver Liganden für Proteinoberflächen. Hier wird eine Strategie beschrieben, um hoch wirksame und spezifische „Miniaturprotein-Liganden“ für die humanen Proteine Bcl-2 und Bcl-XL zu entdecken. Miniaturproteine (siehe Bild) könnten verwendet werden, um einzelne Proteinfunktionen zu untersuchen, sie zu modulieren oder zu analysieren, unabhängig von allen anderen Funktionen des Proteins.

10.1002/1521-3757(20011015)113:20<3922::aid-ange3922>3.0.co;2-8

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Citations (18)