Secondary Structure - 3-10 Helix
Generated by NIH 3D workflows using data provided by
phil.cruz
Created:
3/13/15
Submitted:
3/13/15
Published:
3/13/15
This entry was migrated from the 3D Print Exchange and does not have a .glb file suitable for display in this viewer. You may download the .x3d files from this original entry from the Download button.
The most recent NIH3D processed version which has .glb files is avalilable from the version history.
Category
Description
An alpha helix is a commonly-found protein secondary structure. It is a right-handed coil in which every backbone N-H group donates a hydrogen bond to the C=O group of the amino acid four residues earlier. In the less common 3-10 helix, the bonding occurs at the amino acid three residues earlier, resulting in a tighter helical conformation.
This helix consists of 20 amino acid peptides of poly-L-alanine, and were produced using the peptide builder in Chimera. Phi angle is set at -49.0, and psi angle is set at -26.0.
Download the .pdb file here.