Quantifying end-to-end conformational communication of chirality through an achiral peptide chain

Jonathan Clayden; Alejandro Castellanos; Jordi Solà; Gareth A. Morris

doi:10.1002/anie.200901892

Quantifying end-to-end conformational communication of chirality through an achiral peptide chain

Jonathan Clayden, Alejandro Castellanos, Jordi Solà, Gareth A. Morris

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

Abstract

Successful communication: Two diastereotopic protons more than 60 bonds from the nearest chiral center appear as an AB system, showing that the intervening structure is a well-ordered helix. Decay of anisochronicity quantifies the linear persistence of a helix of achiral amino acids: as little as 3.5 % of the chiral influence is lost with each additional achiral residue. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

Original language	English
Pages (from-to)	5962-5965
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	32
DOIs	https://doi.org/10.1002/anie.200901892
Publication status	Published - 27 Jul 2009

Keywords

Anisochronicity
Conformation analysis
Helicity
NMR spectroscopy
Peptides

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http://www3.interscience.wiley.com/cgi-bin/fulltext/122474149/PDFSTART

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title = "Quantifying end-to-end conformational communication of chirality through an achiral peptide chain",

abstract = "Successful communication: Two diastereotopic protons more than 60 bonds from the nearest chiral center appear as an AB system, showing that the intervening structure is a well-ordered helix. Decay of anisochronicity quantifies the linear persistence of a helix of achiral amino acids: as little as 3.5 \% of the chiral influence is lost with each additional achiral residue. {\textcopyright} 2009 Wiley-VCH Verlag GmbH \& Co. KGaA.",

keywords = "Anisochronicity, Conformation analysis, Helicity, NMR spectroscopy, Peptides",

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AU - Clayden, Jonathan

AU - Castellanos, Alejandro

AU - Solà, Jordi

AU - Morris, Gareth A.

N1 - 478QY Times Cited:0 Cited References Count:41

PY - 2009/7/27

Y1 - 2009/7/27

N2 - Successful communication: Two diastereotopic protons more than 60 bonds from the nearest chiral center appear as an AB system, showing that the intervening structure is a well-ordered helix. Decay of anisochronicity quantifies the linear persistence of a helix of achiral amino acids: as little as 3.5 % of the chiral influence is lost with each additional achiral residue. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

AB - Successful communication: Two diastereotopic protons more than 60 bonds from the nearest chiral center appear as an AB system, showing that the intervening structure is a well-ordered helix. Decay of anisochronicity quantifies the linear persistence of a helix of achiral amino acids: as little as 3.5 % of the chiral influence is lost with each additional achiral residue. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

KW - Anisochronicity

KW - Conformation analysis

KW - Helicity

KW - NMR spectroscopy

KW - Peptides

U2 - 10.1002/anie.200901892

DO - 10.1002/anie.200901892

M3 - Article

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VL - 48

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 32

ER -

Quantifying end-to-end conformational communication of chirality through an achiral peptide chain

Abstract

Keywords

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