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

^*Corresponding author for this work

School of Chemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

94 Citations (Scopus)

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.

Original language	English
Pages (from-to)	5962-5965
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	32
Early online date	30 Jun 2009
DOIs	https://doi.org/10.1002/anie.200901892
Publication status	Published - 27 Jul 2009

Research Groups and Themes

Organic & Biological

Keywords

Anisochronicity
Conformation analysis
Helicity
NMR spectroscopy
Peptides

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10.1002/anie.200901892

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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.",

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author = "Jonathan Clayden and Alejandro Castellanos and Jordi Sol{\`a} and Morris, \{Gareth A.\}",

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T1 - Quantifying end-to-end conformational communication of chirality through an achiral peptide chain

AU - Clayden, Jonathan

AU - Castellanos, Alejandro

AU - Solà, Jordi

AU - Morris, Gareth A.

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.

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.

KW - Anisochronicity

KW - Conformation analysis

KW - Helicity

KW - NMR spectroscopy

KW - Peptides

UR - https://www.scopus.com/pages/publications/70349925664

U2 - 10.1002/anie.200901892

DO - 10.1002/anie.200901892

M3 - Article (Academic Journal)

C2 - 19569153

AN - SCOPUS:70349925664

SN - 1433-7851

VL - 48

SP - 5962

EP - 5965

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

Research Groups and Themes

Keywords

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