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Short Hydrogen Bonds, Circular Dichroism, and Over‐Estimates of Peptide Helicity
Author(s) -
Dang Zhijing,
Hirst Jonathan D.
Publication year - 2001
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 - 10.1002/1521-3773(20011001)40:19<3619::aid-anie3619>3.0.co;2-4
Subject(s) - circular dichroism , helicity , peptide , hydrogen bond , helix (gastropod) , crystallography , vibrational circular dichroism , spectral line , chemistry , physics , nuclear magnetic resonance , biology , particle physics , molecule , quantum mechanics , ecology , snail
More helix than peptide? The helical polypeptides have distinctive circular dichroism (CD) spectra, as shown in the graphic. The recent experimental observation of a peptide with an intense CD spectrum, which suggests a helical content of greater than 100 % is therefore highly anomalous. We present calculations from first principles which could explain this unusual observation.

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