Article (Scientific journals)
beta-lactamases as models for protein-folding studies
Vanhove, M.; Lejeune, Annabelle; Pain, R. H.
1998In Cellular and Molecular Life Sciences, 54 (4), p. 372-377
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Abstract :
[en] This review traces some of the key features of the folding of beta-lactamases and their relevance to the way proteins fold in general. Studies on the enzymes have highlighted the nature and role of equilibrium and transient condensed states. The kinetics of folding are multiphasic, and when monitored by acrylamide quenching of the tryptophan fluorescence, an early phase provides evidence for the transient accumulation of a nonnative intermediate involving burial of tryptophan in a nonpolar environment. Intermediate phases can be understood in terms of progressive folding of different parts of the molecule. The later, slow phases are associated with proline isomerization in the TEM-1 enzyme and, in its P167T mutant form, with isomerization from trans to cis of the E166 T167 peptide bond. Coupled with kinetic and X-ray crystallographic studies of the beta-lactamase from Staphylococcus aureus and its D179Q mutant, it appears that the final stage of folding is that of collapse and packing of the Omega-loop on to the main body of the protein.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Vanhove, M.
Lejeune, Annabelle ;  Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire
Pain, R. H.
Language :
English
Title :
beta-lactamases as models for protein-folding studies
Publication date :
1998
Journal title :
Cellular and Molecular Life Sciences
ISSN :
1420-682X
eISSN :
1420-9071
Publisher :
Birkhäuser, Basel, Switzerland
Volume :
54
Issue :
4
Pages :
372-377
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 14 July 2011

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