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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| Otros Autores: | , , , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Portland Press Ltd
2015
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
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| 008 | 190411s2015 xx ||||fo|||| 00| 0 eng|d | ||
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| 100 | 1 | |a Espada, R. | |
| 245 | 1 | 0 | |a Repeat proteins challenge the concept of structural domains |
| 260 | |b Portland Press Ltd |c 2015 | ||
| 270 | 1 | 0 | |m Ferreiro, D.U.; Protein Physiology Lab., Dep de Química Biológica, Facultad de Ciencias Exactas y Naturales, UBA-CONICET-IQUIBICENArgentina; email: ferreiro@qb.fcen.uba.ar |
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| 506 | |2 openaire |e Política editorial | ||
| 520 | 3 | |a 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. |l eng | |
| 593 | |a Protein Physiology Lab., Dep de Química Biológica, Facultad de Ciencias Exactas y Naturales, UBA-CONICET-IQUIBICEN, Buenos Aires, C1430EGA, Argentina | ||
| 593 | |a Center of Applied Molecular Engineering, Division of Bioinformatics, Department of Molecular Biology, University of Salzburg, Salzburg, 5020, Austria | ||
| 593 | |a Laboratoire de Physique Statistique, CNRS, UPMC, Ecole Normale Supérieure, 24 rue Lhomond, Paris, 75005, France | ||
| 593 | |a Laboratoire de Physique Théorique, CNRS, UPMC, Ecole Normale Supérieure, 24 rue Lhomond, Paris, 75005, France | ||
| 690 | 1 | 0 | |a ANKYRIN-REPEAT |
| 690 | 1 | 0 | |a LOCAL FRUSTRATION |
| 690 | 1 | 0 | |a REPEAT-PROTEIN |
| 690 | 1 | 0 | |a PROTEIN |
| 690 | 1 | 0 | |a REPEAT PROTEIN |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a MOLECULAR EVOLUTION |
| 690 | 1 | 0 | |a PHYSIOLOGICAL PROCESS |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN ANALYSIS |
| 690 | 1 | 0 | |a PROTEIN DOMAIN |
| 690 | 1 | 0 | |a PROTEIN FOLDING |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ANIMAL |
| 690 | 1 | 0 | |a CHEMICAL STRUCTURE |
| 690 | 1 | 0 | |a ENERGY TRANSFER |
| 690 | 1 | 0 | |a HUMAN |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a PROTEIN DOMAIN |
| 690 | 1 | 0 | |a PROTEIN SECONDARY STRUCTURE |
| 690 | 1 | 0 | |a PROTEIN STABILITY |
| 690 | 1 | 0 | |a PROTEIN TERTIARY STRUCTURE |
| 690 | 1 | 0 | |a TANDEM REPEAT |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a ENERGY TRANSFER |
| 690 | 1 | 0 | |a EVOLUTION, MOLECULAR |
| 690 | 1 | 0 | |a HUMANS |
| 690 | 1 | 0 | |a MODELS, MOLECULAR |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a PROTEIN FOLDING |
| 690 | 1 | 0 | |a PROTEIN INTERACTION DOMAINS AND MOTIFS |
| 690 | 1 | 0 | |a PROTEIN STABILITY |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE, SECONDARY |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE, TERTIARY |
| 690 | 1 | 0 | |a REPETITIVE SEQUENCES, AMINO ACID |
| 690 | 1 | 0 | |a TANDEM REPEAT SEQUENCES |
| 700 | 1 | |a Parra, Rodrigo Gonzalo | |
| 700 | 1 | |a Sippl, M.J. | |
| 700 | 1 | |a Mora, T. | |
| 700 | 1 | |a Walczak, A.M. | |
| 700 | 1 | |a Ferreiro, D.U. | |
| 773 | 0 | |d Portland Press Ltd, 2015 |g v. 43 |h pp. 844-849 |p Biochem. Soc. Trans. |x 03005127 |t Biochemical Society Transactions | |
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| 856 | 4 | 0 | |u https://doi.org/10.1042/BST20150083 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_03005127_v43_n_p844_Espada |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03005127_v43_n_p844_Espada |y Registro en la Biblioteca Digital |
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