[1] The non-covalent interactions between the hydrophobic and hydrophilic regions on the polypeptides units help to stabilize the quaternary structure.
Since a protein trimer is composed of multiple polypeptide subunits, it is considered an oligomer.
Multiple copies of a polypeptide encoded by a gene often can form an aggregate referred to as a multimer.
[4] This finding indicated that the distal tail fibers are a multimer of the gene 37 encoded polypeptide.
An analysis of the complementation data further indicated that the polypeptides making up the multimer were folded back on themselves in the form of a hairpin.