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Quantifying End‐to‐End Conformational Communication of Chirality through an Achiral Peptide Chain
Author(s) -
Clayden Jonathan,
Castellanos Alejandro,
Solà Jordi,
Morris Gareth A.
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200901892
Subject(s) - chirality (physics) , residue (chemistry) , stereochemistry , helix (gastropod) , peptide , chemistry , chain (unit) , crystallography , chiral symmetry , biochemistry , physics , biology , ecology , quantum mechanics , astronomy , snail , nambu–jona lasinio model , quark
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.