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dc.contributor.author
Giordano, Daniela
dc.contributor.author
Boubeta, Fernando Martín
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dc.contributor.author
di Prisco, Guido
dc.contributor.author
Estrin, Dario Ariel
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dc.contributor.author
Smulevich, Giulietta
dc.contributor.author
Viappiani, Christiano
dc.contributor.author
Verde, Cinzia
dc.date.available
2021-01-26T13:29:41Z
dc.date.issued
2019-10
dc.identifier.citation
Giordano, Daniela; Boubeta, Fernando Martín; di Prisco, Guido; Estrin, Dario Ariel; Smulevich, Giulietta; et al.; Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins; Mary Ann Liebert; Antioxidants & Redox Signaling; 32; 6; 10-2019; 396-411
dc.identifier.issn
1523-0864
dc.identifier.uri
http://hdl.handle.net/11336/123695
dc.description.abstract
Significance: Temperature is one of the most important drivers in shaping protein adaptations. Many biochemical and physiological processes are influenced by temperature. Proteins and enzymes from organisms living at low temperature are less stable in comparison to high-temperature adapted proteins. The lower stability is generally due to greater conformational flexibility. Recent Advances: Adaptive changes in the structure of cold-adapted proteins may occur at subunit interfaces, distant from the active site, thus producing energy changes associated with conformational transitions transmitted to the active site by allosteric modulation, valid also for monomeric proteins in which tertiary structural changes may play an essential role. Critical Issues: Despite efforts, the current experimental and computational methods still fail to produce general principles on protein evolution, since many changes are protein and species dependent. Environmental constraints or other biological cellular signals may override the ancestral information included in the structure of the protein, thus introducing inaccuracy in estimates and predictions on the evolutionary adaptations of proteins in response to cold adaptation. Future Directions: In this review, we describe the studies and approaches used to investigate stability and flexibility in the cold-adapted globins of the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. In fact, future research directions will be prescient on more detailed investigation of cold-adapted proteins and the role of fluctuations between different conformational states.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Mary Ann Liebert
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
BACTERIAL GLOBIN
dc.subject
HEME-POCKET FLEXIBILITY
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HEXA-COORDINATION
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OXIDATIVE/NITROSATIVE STRESS
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THERMAL ADAPTATION
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-20T14:46:42Z
dc.journal.volume
32
dc.journal.number
6
dc.journal.pagination
396-411
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
New York
dc.description.fil
Fil: Giordano, Daniela. Institute Of Biosciences And Bioresources; Italia
dc.description.fil
Fil: Boubeta, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: di Prisco, Guido. Institute Of Biosciences And Bioresources; Italia
dc.description.fil
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Smulevich, Giulietta. Firenze University; Italia
dc.description.fil
Fil: Viappiani, Christiano. Università di Parma; Italia
dc.description.fil
Fil: Verde, Cinzia. Institute Of Biosciences And Bioresources; Italia
dc.journal.title
Antioxidants & Redox Signaling
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.liebertpub.com/doi/10.1089/ars.2019.7887
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1089/ars.2019.7887
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