The energy landscapes of repeat-containing proteins: topology, cooperativity, and the folding funnels of one-dimensional architectures.
Repeat-proteins are made up of near repetitions of 20- to 40-amino acid stretches.These polypeptides usually fold up into non-globular, elongated architectures that are stabilized by the interactions within animed aniflex complete each repeat and those between adjacent repeats, but that lack contacts between residues distant in sequence.The inheren