TY - JOUR
T1 - Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study
AU - Solà, Jordi
AU - Helliwell, Madeleine
AU - Clayden, Jonathan
PY - 2011/1
Y1 - 2011/1
N2 - 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. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62-69, 2011.
AB - 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. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62-69, 2011.
UR - https://www.ccdc.cam.ac.uk/structures/search?id=doi:10.5517/ccv60vw&sid=DataCite
U2 - 10.1002/bip.21535
DO - 10.1002/bip.21535
M3 - Article
SN - 0006-3525
VL - 95
SP - 62
EP - 69
JO - Biopolymers
JF - Biopolymers
IS - 1
ER -