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dc.contributor.author
Marchetti, Julia
dc.contributor.author
Monzón, Alexander
dc.contributor.author
Tosatto, Silvio C.E.
dc.contributor.author
Parisi, Gustavo Daniel
dc.contributor.author
Fornasari, Maria Silvina
dc.date.available
2021-06-04T18:18:17Z
dc.date.issued
2019-03-15
dc.identifier.citation
Marchetti, Julia; Monzón, Alexander; Tosatto, Silvio C.E.; Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 431; 6; 15-3-2019; 1298-1307
dc.identifier.issn
0022-2836
dc.identifier.uri
http://hdl.handle.net/11336/133240
dc.description.abstract
The conformations accessible to proteins are determined by the inter-residue interactions between amino acid residues. During evolution, structural constraints that are required for protein function providing biologically relevant information can exist. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered and disordered proteins. Using a structurally constrained model of protein evolution, we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~ 68% are in disordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~ 11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Academic Press Ltd - Elsevier Science Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CONFORMATIONAL DIVERSITY
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DISORDERED PROTEINS
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PROTEIN ENSEMBLE
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PROTEIN EVOLUTION
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Biología
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-11T12:33:21Z
dc.journal.volume
431
dc.journal.number
6
dc.journal.pagination
1298-1307
dc.journal.pais
Reino Unido
dc.description.fil
Fil: Marchetti, Julia. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Università di Padova; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Tosatto, Silvio C.E.. Università di Padova; Italia
dc.description.fil
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Journal of Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.jmb.2019.01.031
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0022283619300488
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