Mostrar el registro sencillo del ítem

dc.contributor.author
Nolan, María Verónica
dc.contributor.author
Sanchez, Julieta Maria
dc.contributor.author
Perillo, Maria Angelica
dc.date.available
2018-03-09T17:44:49Z
dc.date.issued
2015-12
dc.identifier.citation
Nolan, María Verónica; Sanchez, Julieta Maria; Perillo, Maria Angelica; PEG-induced molecular crowding leads to a relaxed conformation, higher thermal stability and lower catalytic efficiency of Escherichia coli β-galactosidase; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 136; 12-2015; 1202-1206
dc.identifier.issn
0927-7765
dc.identifier.uri
http://hdl.handle.net/11336/38421
dc.description.abstract
Enzymatic activities were historically assayed in dilute solutions where molecular crowding, molecular confinement and their consequences were not taken into account. Here we report how macromolecular crowding tunes catalytic parameters for the tetrameric β-Galactosidase from Escherichia coli, β-Gal. We detected increases in KM (weaker substrate binding) and a nonlinear variation in Vmax, with a minimum at 25% W/P of the crowding agent (polyethyleneglycol molecular mass 6000, PEG6000) resulting in a linear decrease in the catalytic efficiency (kcat/KM) within the whole [PEG6000] range tested). Presence of crowding agent affected β-Gal structural content and increased its thermal resistance. Steady state fluorescence and Fourier transformed infrared spectroscopic observations are compatible with crowding-induced disordering and restricted internal dynamics as a result of excluded volume and solvent structuring effects. This leads to a non-optimal substrate-binding site and a less conformationally strained protein.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Enzymatic Activity
dc.subject
Peg-Induced Molecular Crowding
dc.subject
Protein Structure
dc.subject
Thermal Stability
dc.subject
Water Activity
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
PEG-induced molecular crowding leads to a relaxed conformation, higher thermal stability and lower catalytic efficiency of Escherichia coli β-galactosidase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-07T18:39:57Z
dc.journal.volume
136
dc.journal.pagination
1202-1206
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Nolan, María Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
dc.description.fil
Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
dc.description.fil
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
dc.journal.title
Colloids and Surfaces B: Biointerfaces
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.colsurfb.2015.11.003
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927776515302861


Archivos asociados

Documento no disponible

Comunidades y colecciones

  • Articulos(IIBYT) [414]
    Articulos de INSTITUTO DE INVESTIGACIONES BIOLOGICAS Y TECNOLOGICAS

Mostrar el registro sencillo del ítem