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

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

31 Scopus citations

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	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

ASJC Scopus subject areas

Catalysis
General Chemistry

Access to Document

10.1002/anie.201303900

Cite this

@article{8995d72ffe854e3c95265e7cd6b8bc3c,

title = "A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry",

abstract = "Stable and reactive: A crystal structure at 1.35{\AA} 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.",

keywords = "coiled coils, depsipeptides, dynamic chemistry, peptide networks, thiodepsipeptides",

author = "Zehavit Dadon and Manickasundaram Samiappan and Anat Shahar and Raz Zarivach and Gonen Ashkenasy",

year = "2013",

month = sep,

day = "16",

doi = "10.1002/anie.201303900",

language = "English",

volume = "52",

pages = "9944--9947",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

number = "38",

}

TY - JOUR

T1 - A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry

AU - Dadon, Zehavit

AU - Samiappan, Manickasundaram

AU - Shahar, Anat

AU - Zarivach, Raz

AU - Ashkenasy, Gonen

PY - 2013/9/16

Y1 - 2013/9/16

N2 - 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.

AB - 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.

KW - coiled coils

KW - depsipeptides

KW - dynamic chemistry

KW - peptide networks

KW - thiodepsipeptides

UR - https://www.scopus.com/pages/publications/84884260963

U2 - 10.1002/anie.201303900

DO - 10.1002/anie.201303900

M3 - Article

C2 - 23929823

AN - SCOPUS:84884260963

SN - 1433-7851

VL - 52

SP - 9944

EP - 9947

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 38

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this