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Biochem Soc Trans. 2015 Oct;43(5):844-9. doi: 10.1042/BST20150083.

Repeat proteins challenge the concept of structural domains.

Author information

1
Protein Physiology Lab, Dep de Química Biológica, Facultad de Ciencias Exactas y Naturales, UBA-CONICET-IQUIBICEN, Buenos Aires, C1430EGA, Argentina.
2
Center of Applied Molecular Engineering, Division of Bioinformatics, Department of Molecular Biology, University of Salzburg, 5020 Salzburg, Austria.
3
Laboratoire de physique statistique, CNRS, UPMC and Ecole normale supérieure, 24 rue Lhomond, 75005 Paris, France.
4
Laboratoire de physique théorique, CNRS, UPMC and Ecole normale supérieure, 24 rue Lhomond, 75005 Paris, France.
5
Protein Physiology Lab, Dep de Química Biológica, Facultad de Ciencias Exactas y Naturales, UBA-CONICET-IQUIBICEN, Buenos Aires, C1430EGA, Argentina ferreiro@qb.fcen.uba.ar.

Abstract

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.

KEYWORDS:

ankyrin-repeat; local frustration; repeat-protein

PMID:
26517892
DOI:
10.1042/BST20150083
[Indexed for MEDLINE]

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