Examples of polypeptide

• 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.

• Renaturation of polypeptide chains to the original or near-original shape may only be possible by such treatments as heating.

• It appears, at least in the case of spinach ferredoxin, that cluster insertion is a prerequisite for the polypeptide to fold properly.

• Getting greasy : how transmembrane polypeptide segments integrate into the lipid bilayer.

• Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides.

• The presence of the cofactor is sometimes essential for the polypeptide to fold.

• Thus, a polypeptide folding in this encapsulated environment simply has no other species with which to form a multimolecular aggregate.

• Reactions are, therefore, non-adiabatic and the essential electronic interaction between redox cofactors must be mediated by the polypeptide matrix.