Show simple item record

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
dc.conicet.fuente individual


Archivos asociados

Icon
Blocked Acceso no disponible

This item appears in the following Collection(s)

  • Articulos(IIBYT) [360]
    Articulos de INSTITUTO DE INVESTIGACIONES BIOLOGICAS Y TECNOLOGICAS

Show simple item record

info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Atribución-NoComercial-SinDerivadas 2.5 Argentina (CC BY-NC-ND 2.5 AR)