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Updated: Jun 12, 2026

Identification of Fatty Acids in Bacillus cereus
Published on: December 5, 2016
1H, 13C and 15N backbone resonance assignments for the BS3 class A β-lactamase from Bacillus licheniformis
Julie Vandenameele1, André Matagne, Christian Damblon
1Laboratoire d'Enzymologie et Repliement des protéines, Centre d'Ingénierie des Protéines, Institut de Chimie B6, Université de Liège, 4000, Liège (Sart-Tilman), Belgium. Julie.Vandenameele@ulg.ac.be
Abstract:
Class A β-lactamases (260-280 amino acids; M ( r ) ~ 29,000) are among the largest proteins studied in term of their folding properties. They are composed of two structural domains: an all-α domain formed by five to eight helices and an α/β domain consisting of a five-stranded antiparallel β-sheet covered by three to four α-helices. The α domain (~150 residues) is made up of the central part of the polypeptide chain whereas the α/β domain (111-135 residues) is constituted by the N- and C-termini of the protein. Our goal is to determine in which order the different secondary structure elements are formed during the folding of BS3. With this aim, we will use pulse-labelling hydrogen/deuterium exchange experiments, in combination with 2D-NMR measurements, to monitor the time-course of formation and stabilization of secondary structure elements. Here we report the backbone resonance assignments as the requirement for further hydrogen/deuterium exchange studies.
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