Artículo
Equilibrium partially folded states of B. licheniformis β -lactamase
Fecha de publicación:
30/03/2019
Editorial:
Springer
Revista:
European Biophysics Journal With Biophysics Letters
ISSN:
0175-7571
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
훽-Lactamases (penicillinases) facilitate bacterial resistance to antibiotics and are excellent theoretical and experimental models in protein structure, dynamics and evolution. Bacillus licheniformis exo-small penicillinase (ESP) is a Class A 훽 -lactamase with three tryptophan residues located one in each of its two domains and one in the interface between domains. The conformational landscape of three well-characterized ESP Trp→Phe mutants was characterized in equilibrium unfolding experiments by measuring tryptophan fuorescence, far-UV CD, activity, hydrodynamic radius, and limited proteolysis. The Trp→Phe substitutions had little impact on the native conformation, but changed the properties of the partially folded states populated at equilibrium. The results were interpreted in the framework of modern theories of protein folding.
Palabras clave:
CIRCULAR DICHROISM
,
PROTEIN CONFORMATION
,
PROTEIN FOLDING
,
Β-LACTAMASE
Archivos asociados
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Identificadores
Colecciones
Articulos(IMBICE)
Articulos de INST.MULTIDISCIPL.DE BIOLOGIA CELULAR (I)
Articulos de INST.MULTIDISCIPL.DE BIOLOGIA CELULAR (I)
Citación
Risso, Valeria Alejandra; Ermacora, Mario Roberto; Equilibrium partially folded states of B. licheniformis β -lactamase; Springer; European Biophysics Journal With Biophysics Letters; 48; 4; 30-3-2019; 341-348
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