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Hydrogen‐Bond Lengths in Polypeptide Helices: No Evidence for Short Hydrogen Bonds
Author(s) -
Aravinda Subrayashastry,
Datta Saumen,
Shamala Narayanaswamy,
Balaram Padmanabhan
Publication year - 2004
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.200461127
Subject(s) - hydrogen bond , helix (gastropod) , crystallography , bond length , circular dichroism , chemistry , hydrogen , crystal structure , molecule , biology , ecology , organic chemistry , snail
The long and the short of it : N⋅⋅⋅O distances less than 2.8 Å (see picture) have been implicated in determining the 220 nm circular dichroism band intensity in helical peptides. An analysis of helical peptide crystal structures, however, reveals the average experimentally determined hydrogen‐bond lengths are 2.978–3.113 Å (α helix) and 2.907–3.211 Å (3 10 helix).