IQUIFIB 02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Probing the structure of partially folded states of B. licheniformis Ò-lactamase by cysteine mutagenesis.
Autor/es:
VALERIA A. RISSO; JAVIER SANTOS; MAURICIO P. SICA; MARIO R. ERMÁCORA
Lugar:
Rio de Janeiro Brasil
Reunión:
Workshop; Workshop on Biocalorimetry and Biological Thermodynamics; 2006
Resumen:
The 256-residue protein B. licheniformis exo-small B lactamese (ESBL) has two nonsequential domains and a complex architecture. To study the conformation of partially folded states of ESBL, variants were prepared replacing serine at position 126 and/or 265 with cysteine, so that introducing thiol groups in buried regions of each ESBL domain (abstract is truncated).
