Structure in sequence

April 16th, 2018 by Yiyun Song

Structure in sequence

Structure in sequence, Published online: 16 April 2018; doi:10.1038/s41589-018-0050-3

Structure in sequence

Dynamic coupling between conformations and nucleotide states in DNA gyrase

April 16th, 2018 by Aakash Basu

Dynamic coupling between conformations and nucleotide states in DNA gyrase

Dynamic coupling between conformations and nucleotide states in DNA gyrase, Published online: 16 April 2018; doi:10.1038/s41589-018-0037-0

Single-molecule measurements of DNA gyrase activity reveal conformational dynamics coupling ATP consumption to DNA supercoiling.
  • Posted in Nat Chem Biol, Publications
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Designing macrocyclic disulfide-rich peptides for biotechnological applications

April 16th, 2018 by Conan K. Wang

Designing macrocyclic disulfide-rich peptides for biotechnological applications

Designing macrocyclic disulfide-rich peptides for biotechnological applications, Published online: 16 April 2018; doi:10.1038/s41589-018-0039-y

Through molecular grafting, cyclic disulfide-rich peptides can be used as scaffolds to improve the stability, rigidity, and cellular uptake of bioactive peptides, although a number of factors should be considered when designing such grafted peptides.
  • Posted in Nat Chem Biol, Publications
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Understanding the Pro/N-end rule pathway

April 16th, 2018 by David A. Dougan

Understanding the Pro/N-end rule pathway

Understanding the Pro/N-end rule pathway, Published online: 16 April 2018; doi:10.1038/s41589-018-0045-0

Regulated destruction of proteins underlies just about everything a cell does. A structural study of human Gid4, the N-recognin of the Pro/N-end rule pathway that targets proteins through their N-terminal proline, illuminates the recognition of substrates by this proteolytic system.

[ASAP] Second-Shell Hydrogen Bond Impacts Transition-State Structure in <italic toggle=”yes”>Bacillus subtilis</italic> Oxalate Decarboxylase

April 11th, 2018 by Wen Zhu, Laurie A. Reinhardt, Nigel G. J. Richards

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.8b00214

Author Correction: Mitochondrial DNA repair and replication proteins revealed by targeted chemical probes

April 2nd, 2018 by Simon Wisnovsky

Author Correction: Mitochondrial DNA repair and replication proteins revealed by targeted chemical probes

Author Correction: Mitochondrial DNA repair and replication proteins revealed by targeted chemical probes, Published online: 02 April 2018; doi:10.1038/s41589-018-0040-5

Author Correction: Mitochondrial DNA repair and replication proteins revealed by targeted chemical probes
  • Posted in Nat Chem Biol, Publications
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FINO<sub>2</sub> initiates ferroptosis through GPX4 inactivation and iron oxidation

April 2nd, 2018 by Michael M. Gaschler

FINO2 initiates ferroptosis through GPX4 inactivation and iron oxidation

FINO<sub>2</sub> initiates ferroptosis through GPX4 inactivation and iron oxidation, Published online: 02 April 2018; doi:10.1038/s41589-018-0031-6

FINO2 is a small molecule that requires the endoperoxide moiety and hydroxyl group to promote ferroptosis through indirect inhibition of GPX4 enzymatic function and direct oxidation of iron, resulting in increased lipid peroxidation.
  • Posted in Nat Chem Biol, Publications
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Super-long single-molecule tracking reveals dynamic-anchorage-induced integrin function

April 2nd, 2018 by Taka A. Tsunoyama

Super-long single-molecule tracking reveals dynamic-anchorage-induced integrin function

Super-long single-molecule tracking reveals dynamic-anchorage-induced integrin function, Published online: 02 April 2018; doi:10.1038/s41589-018-0032-5

Dissolved oxygen and a reducing-plus-oxidizing system suppress photobleaching and photoblinking in single-molecule tracking experiments, allowing long recordings of CD47 and integrin that showed temporary immobilization within focal adhesions.
  • Posted in Nat Chem Biol, Publications
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The structural organization of substrate loading in iterative polyketide synthases

April 2nd, 2018 by Dominik A. Herbst

The structural organization of substrate loading in iterative polyketide synthases

The structural organization of substrate loading in iterative polyketide synthases, Published online: 02 April 2018; doi:10.1038/s41589-018-0026-3

The crystal structure and cryo-electron microscopy of the loading/condensing region of a nonreducing polyketide synthase reveals the insertion of a starter-unit acyltransferase into the condensing region and an asymmetrical post-loading state.
  • Posted in Nat Chem Biol, Publications
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[ASAP] Structural Determinants for the Interactions of Chemically Modified Nucleic Acids with the Stabilin-2 Clearance Receptor

March 29th, 2018 by Hans Gaus, Colton M. Miller, Punit P. Seth, Edward N. Harris

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.8b00126