A more systematic method classifies them into different "fold groups" based on the overall shape of the protein backbone in the folded domain.

This directionality is sometimes used in preliminary, low-resolution electron-density maps to determine the direction of the protein backbone.

The method used a fast, crude docking model phase using only the protein backbone.

Potential points of attachment include the terminal amino group of the protein backbone and the side chain of cysteine residues.

This method classifies zinc finger proteins into "fold groups" based on the overall shape of the protein backbone in the folded domain.

This allows a novel sequence to be designed onto a given protein backbone.

This process is determined by the structure of the protein backbone and the carbohydrate attachment site.

The other two dihedral angles in the peptide bond determine the local shape assumed by the protein backbone.

A hairpin is a special case of a turn, in which the direction of the protein backbone reverses and the flanking secondary structure elements interact.

The phosphate is bound to the protein backbone through serine or threonine amino acid residues.