Quantifying End‐to‐End Conformational Communication of Chirality through an Achiral Peptide Chain | Zendy

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

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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.

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