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dc.contributor.author
Santos, Javier
dc.contributor.author
Gebhard, Leopoldo German
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Risso, Valeria Alejandra
dc.contributor.author
Ferreyra, Raul Gabriel
dc.contributor.author
Rossi, Juan Pablo Francisco
dc.contributor.author
Ermacora, Mario Roberto
dc.date.available
2018-04-10T17:14:09Z
dc.date.issued
2004-02
dc.identifier.citation
Santos, Javier; Gebhard, Leopoldo German; Risso, Valeria Alejandra; Ferreyra, Raul Gabriel; Rossi, Juan Pablo Francisco; et al.; Folding of an Abridged β-Lactamase; American Chemical Society; Biochemistry; 43; 6; 2-2004; 1715-1723
dc.identifier.issn
0006-2960
dc.identifier.uri
http://hdl.handle.net/11336/41522
dc.description.abstract
The effects of C-terminal truncation on the equilibrium folding transitions and folding kinetics of B. licheniformis exo small β−lactamase (ES-βL) have been measured. ES-βL lacking 19 residues (ES-βLCΔ19) has no enzymic activity. Deletion of the last 14 residues produces ES-βLCΔ14, which is 0.1% active. The enzyme lacking nine residues (ES-βLCΔ9) is nearly fully active, has native optical and hydrodynamic properties, and is protease resistant, a distinguishing feature of the wild-type enzyme. Although ES-βLCΔ9 folds properly, it does so 4 orders of magnitude slower than ES-βL, making possible the isolation and characterization of a compact intermediate state (IP ES-βLCΔ9). Based on the analysis of folding rates and equilibrium constants, we propose that equilibrium between IP ES-βLCΔ9 and other intermediate slow folding. Residues removed in ES-βLCΔ9 and ES-βLCΔ14 are helical and firmly integrated into the enzyme body through many van der Waals interactions involving residues distant in sequence. The results suggest that the deleted residues play a key role in the folding process and also the existence of a modular organization of the protein matrix, at the subdomain level. The results are compared with other examples of this kind in the folding literature.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject.classification
Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Folding of an Abridged β-Lactamase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-04-10T13:50:17Z
dc.journal.volume
43
dc.journal.number
6
dc.journal.pagination
1715-1723
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Santos, Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Gebhard, Leopoldo German. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Risso, Valeria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
dc.description.fil
Fil: Ferreyra, Raul Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
dc.description.fil
Fil: Rossi, Juan Pablo Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
dc.description.fil
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
dc.journal.title
Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bi0358162
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/bi0358162
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