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dc.contributor.author
Zea, Diego Javier
dc.contributor.author
Monzón, Alexander
dc.contributor.author
Gonzalez, Claudia
dc.contributor.author
Fornasari, Maria Silvina
dc.contributor.author
Tosatto, Silvio C. E.
dc.contributor.author
Parisi, Gustavo Daniel
dc.date.available
2017-09-04T20:11:01Z
dc.date.issued
2016-04
dc.identifier.citation
Zea, Diego Javier; Monzón, Alexander; Gonzalez, Claudia; Fornasari, Maria Silvina; Tosatto, Silvio C. E.; et al.; Disorder transitions and conformational diversity cooperatively modulate biological function in proteins; Wiley Blackwell Publishing, Inc; Protein Science; 25; 6; 4-2016; 1138-1146
dc.identifier.issn
0961-8368
dc.identifier.uri
http://hdl.handle.net/11336/23621
dc.description.abstract
Structural differences between conformers sustain protein biological function. Here, we studied in a large dataset of 745 intrinsically disordered proteins, how ordered-disordered transitions modulate structural differences between conformers as derived from crystallographic data. We found that almost 50% of the proteins studied show no transitions and have low conformational diversity while the rest show transitions and a higher conformational diversity. In this last subset, 60% of the proteins become more ordered after ligand binding, while 40% more disordered. As protein conformational diversity is inherently connected with protein function our analysis suggests differences in structure-function relationships related to order-disorder transitions.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Disorder
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Conformational Diversity
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Protein Function
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Transitions
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Disorder transitions and conformational diversity cooperatively modulate biological function in proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-08-29T15:39:00Z
dc.identifier.eissn
1469-896X
dc.journal.volume
25
dc.journal.number
6
dc.journal.pagination
1138-1146
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Hoboken
dc.description.fil
Fil: Zea, Diego Javier. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Monzón, Alexander. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Gonzalez, Claudia. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Tosatto, Silvio C. E.. Università di Padova; Italia
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Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Protein Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/pro.2931/abstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1002/pro.2931
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