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Article

Effects of serine-to-cysteine mutations on beta-lactamase folding.

Biophysical journal - 1 Sept 2007

Santos Javier, Risso Valeria A, Sica Mauricio P, Ermácora Mario R

Abstract excerpt

B. licheniformis exo-small beta-lactamase (ESBL) has two nonsequential domains and a complex architecture. We replaced ESBL serine residues 126 and 265 with cysteine to probe the conformation of buried regions in each domain. Spectroscopic, hydrodynamic, and chemical methods revealed that the mutations do not alter the native fold but distinctly change stability (S-126C > wild-type > S-126/265C > S-265C ESBL) and...

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Identifiers

PMID: 17496026
DOI: 10.1529/biophysj.106.103804
PMCID: PMC1948053

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Source receipt: pubmed, retrieved 7 Sept 2026.

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