Repeat proteins challenge the concept of structural domains

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 co-operate in stabilizing structural forms that comprise several repeat-units. For ma...

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Autor principal: Espada, R.
Otros Autores: Parra, Rodrigo Gonzalo, Sippl, M.J, Mora, T., Walczak, A.M, Ferreiro, D.U
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Portland Press Ltd 2015
Acceso en línea:Registro en Scopus
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Sumario: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 co-operate 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 breakdown of co-operativity and the appearance of folding sub-domains within an apparently regular repeat array. The quasi-1D 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 behaviour of these ubiquitous biological systems. © 2015 Authors; published by Portland Press Limited.
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ISSN:03005127
DOI:10.1042/BST20150083