Biological polymers such as a polypeptide chain are heteropolymers where each segment is different.
The large oligosaccharide is transferred en bloc to the nascent polypeptide chain, which is transported across or inserted into the rough endoplasmic reticulum membrane.
This is associated with the release of polypeptide from the apical binding surface into the cavity and the commencement of folding.
In a cross-b motif, the hydrogen bonding capacity of the polypeptide backbone can be fully utilized.
This reinforces the concept that the immune system of each host recognizes different polypeptide bands.
Configuration of polypeptide chains with favoured orientation around single bonds : two new pleated sheets.
The force field is then refined for a given polypeptide structure in order to match the calculated frequencies with the experiment.
The wide association of the cross- structure seems to indicate that this molecular structure is a stable and accessible conformation for many polypeptide chains.
