The enigma of the near-symmetry of proteins: Domain swapping.

ABSTRACT: The majority of proteins form oligomers which have rotational symmetry. Literature has suggested many functional advantages that the symmetric packing offers. Yet, despite these advantages, the vast majority of protein oligomers are only nearly symmetric. A key question in the field of proteins structure is therefore, if symmetry is so advantageous, why do oligomers settle for aggregates that do not maximize that structural property? The answer to that question is apparently multi-parametric, and involves distortions at the interaction zones of the monomer units of the oligomer in order to minimize the free energy, the dynamics of the protein, the effects of surroundings parameters, and the mechanism of oligomerization. The study of this problem is in its infancy: Only the first parameter

SUBMITTER: Bonjack-Shterengartz M 

PROVIDER: S-EPMC5510828 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature