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Interruption of a 3 10 ‐helix by a single Gly residue in a poly‐Aib motif: A crystallographic study
Author(s) -
Solà Jordi,
Helliwell Madeleine,
Clayden Jonathan
Publication year - 2011
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21535
Subject(s) - chemistry , residue (chemistry) , crystallography , solid state , helix (gastropod) , structural motif , stereochemistry , biochemistry , ecology , snail , biology
The structural influence of a single Gly residue inserted into an Aib 16 homooligomer was studied in the solid state by X‐ray crystallography. The peptides N 3 Aib 8 GlyAib 8 PheNH 2 ( 1 ) and CbzPheAib 8 GlyAib 8 ( 2 ) were found to adopt well‐defined helical structures, which are broadly 3 10 helical. Indeed, 2 is the longest crystallographic 3 10 helix thus far reported. However, in the region of the central Gly residue, a loosening of the 3 10 structure is observed in both peptides, with 1 clearly showing local adoption of an α‐helical structure in the region of residues 7–9. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62–69, 2011.