A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry

Zehavit Dadon; Manickasundaram Samiappan; Anat Shahar; Raz Zarivach; Gonen Ashkenasy

doi:10.1002/anie.201303900

A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry

Zehavit Dadon, Manickasundaram Samiappan, Anat Shahar, Raz Zarivach, Gonen Ashkenasy

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

Abstract

Stable and reactive: A crystal structure at 1.35Å of a thioester coiled-coil protein reveals high similarity to all-peptide-bond proteins. In these assemblies, the thioester bonds are kept reactive towards thiol molecules in the mixture. This enables efficient domain exchange between proteins in response to changes in folding conditions or introduction of external templates.

Original language	American English
Pages (from-to)	9944-9947
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	38
DOIs	https://doi.org/10.1002/anie.201303900
State	Published - 16 Sep 2013

Keywords

coiled coils
depsipeptides
dynamic chemistry
peptide networks
thiodepsipeptides

All Science Journal Classification (ASJC) codes

General Chemistry
Catalysis

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10.1002/anie.201303900

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A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry

Abstract

Keywords

All Science Journal Classification (ASJC) codes

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