Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study

Jordi Solà, Madeleine Helliwell, Jonathan Clayden*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

23 Citations (Scopus)

Abstract

The structural influence of a single Gly residue inserted into an Aib16 homooligomer was studied in the solid state by X-ray crystallography. The peptides N3Aib8GlyAib8PheNH2 (1) and CbzPheAib8GlyAib8 (2) were found to adopt well-defined helical structures, which are broadly 310 helical. Indeed, 2 is the longest crystallographic 310 helix thus far reported. However, in the region of the central Gly residue, a loosening of the 310 structure is observed in both peptides, with 1 clearly showing local adoption of an α-helical structure in the region of residues 7-9.

Original languageEnglish
Pages (from-to)62-69
Number of pages8
JournalBiopolymers
Volume95
Issue number1
Early online date19 Aug 2010
DOIs
Publication statusPublished - Jan 2011

Fingerprint

Dive into the research topics of 'Interruption of a 3<sub>10-</sub>helix by a single Gly residue in a poly-Aib motif: A crystallographic study'. Together they form a unique fingerprint.

Cite this