Directed evolution of a synthetic phylogeny of programmable Trp repressors

February 26th, 2018 by Jared W. Ellefson

Directed evolution of a synthetic phylogeny of programmable Trp repressors

Directed evolution of a synthetic phylogeny of programmable Trp repressors, Published online: 26 February 2018; doi:10.1038/s41589-018-0006-7

Directed evolution of Trp repressor (TrpR) variants that are responsive to halogenated tryptophan analogs and recognize new operator sites serve as useful components for constructing complex gene expression networks.
  • Posted in Nat Chem Biol, Publications
  • Comments Off on Directed evolution of a synthetic phylogeny of programmable Trp repressors

Trp-ing upon new repressors

February 26th, 2018 by Andreas K. Brödel

Trp-ing upon new repressors

Trp-ing upon new repressors, Published online: 26 February 2018; doi:10.1038/s41589-018-0012-9

Bioengineers have used directed evolution to generate a new family of synthetic transcription factors based on the tryptophan repressor. The evolved repressor family enables researchers to build new gene circuits for biomedical applications.

Sequential Protein Expression and Capsid Assembly in Cell: Toward the Study of Multiprotein Viral Capsids Using Solid-State Nuclear Magnetic Resonance Techniques

February 23rd, 2018 by Sébastien Alphonse, Boris Itin, Reza Khayat and Ranajeet Ghose

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.8b00003

Call for Nominations — ACS Infectious Disease Young Investigator Award

February 22nd, 2018 by pthomas2

 

 

 

 

 

 

 

 

Nominations for the  2018 ACS Infectious Diseases Young Investigator Awards  are now open (deadline:  March 1, 2018)  Nominations should be submitted to:  https://acspubs.formstack.com/forms/2018_acsinfectious_lectureship

Protein Plasticity and Peptide Editing in the MHC I Antigen Processing Pathway

February 22nd, 2018 by Tim Elliott and Andy van Hateren

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.7b01307

Orthogonal Information Encoding in Living Cells with High Error-Tolerance, Safety, and Fidelity

February 21st, 2018 by Lifu Song and An-Ping Zeng

TOC Graphic

ACS Synthetic Biology
DOI: 10.1021/acssynbio.7b00382

More Than a Light Switch: Engineering Unconventional Fluorescent Configurations for Biological Sensing

February 20th, 2018 by William J. Peveler and W. Russ Algar

TOC Graphic

ACS Chemical Biology
DOI: 10.1021/acschembio.7b01022
  • Posted in ACS Chemical Biology, Publications
  • Comments Off on More Than a Light Switch: Engineering Unconventional Fluorescent Configurations for Biological Sensing

Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases

February 19th, 2018 by Lukas Reisky

Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases

Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases, Published online: 19 February 2018; doi:10.1038/s41589-018-0005-8

The discovery of cytochrome P450 monooxygenases that catalyze oxidative demethylation of 6-O-methyl-d-galactose reveals a new activity of cytochrome P450 enzymes and their role in polysaccharide biomass degradation in marine bacteria.
  • Posted in Nat Chem Biol, Publications
  • Comments Off on Oxidative demethylation of algal carbohydrates by cytochrome P450 monooxygenases

Altering form for function

February 14th, 2018 by Nature Chemical Biology - Issue - nature.com science feeds

Altering form for function

Altering form for function, Published online: 14 February 2018; doi:10.1038/nchembio.2582

Elucidating the mechanisms by which biomolecules are chemically modified and how these alterations regulate biological pathways represents a leading frontier in chemical biology.

Protein evolution: Hacking an enzyme

February 14th, 2018 by Kristoffer E Johansson

Protein evolution: Hacking an enzyme

Protein evolution: Hacking an enzyme, Published online: 14 February 2018; doi:10.1038/nchembio.2574

Early stages of protein evolution are inherently difficult to study. Genetic selection in Escherichia coli has now identified a life-sustaining de novo enzyme arising from a simple scaffold that is completely different from the native enzyme.