Reactions are, therefore, non-adiabatic and the essential electronic interaction between redox cofactors must be mediated by the polypeptide matrix.
Thus, a polypeptide folding in this encapsulated environment simply has no other species with which to form a multimolecular aggregate.
The presence of the cofactor is sometimes essential for the polypeptide to fold.
Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides.
Getting greasy : how transmembrane polypeptide segments integrate into the lipid bilayer.
It appears, at least in the case of spinach ferredoxin, that cluster insertion is a prerequisite for the polypeptide to fold properly.
Renaturation of polypeptide chains to the original or near-original shape may only be possible by such treatments as heating.
The wide association of the cross- structure seems to indicate that this molecular structure is a stable and accessible conformation for many polypeptide chains.
