Repeat Proteins challenge the concept of structural domains

ESPADA, R; PARRA, RG; SIPPL M; MORA, T; WALCZAK, AM; FERREIRO, DU

BIOCHEMICAL SOCIETY TRANSACTIONS

PORTLAND PRESS LTD

Lugar: Londres; Año: 2015

0300-5127

Structural domains are believed to be modules within proteins that can fold and function independently. Some proteins show tandem repetitions of apparent modular structure that do not fold independently, but rather cooperate in stabilizing structural forms that comprise several repeat-units. For many natural repeat-proteins it has been shown that weak energetic links between repeats lead to the break down of cooperativity and the appearance of folding sub- domains within an apparently regular repeat array. The quasi-one-dimensional architecture of repeat-proteins is crucial in detailing how the local energetic balances can modulate the folding dynamics of these proteins, which can be related to the physiological behavior of these ubiquitous biological systems.