Reference : Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Di Paolo, Alexandre mailto [Université de Liège - ULg > Sciences de la Vie > Enzymologie et Repliement des Protéine, Centre d'ingénierie des protéines > >]
Duval, Valerie [Université de Liège - ULg > Centre d'ingénierie des protéines > > >]
Matagne, André mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Redfield, Christina mailto [University of Oxford > Department of Biochemistry > > >]
Biomolecular NMR assignments
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[en] Backbone resonance assignments ; lysozyme ; protein folding
[en] Lysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two structural domains connected by a helix, and has its catalytic residues located at the interface between these two domains. An interesting feature of lambda lysozyme, when compared to the well-characterised hen egg-white lysozyme, is its lack of disulfide bridges; this makes lambda lysozyme an interesting system for studies of protein folding. A comparison of the folding properties of lambda lysozyme and hen lysozyme will provide important insights into the role that disulfide bonds play in the refolding pathway of the latter protein. Here we report the (1)H, (13)C and (15)N backbone resonance assignments for lambda lysozyme by heteronuclear multidimensional NMR spectroscopy. These assignments provide the starting point for detailed investigation of the refolding pathway using pulse-labelling hydrogen/deuterium exchange experiments monitored by NMR.

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