Reference : Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/14572
Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
English
Di Paolo, Alexandre mailto [Université de Liège - ULg > Sciences de la Vie > Enzymologie et Repliement des Protéine, Centre d'ingénierie des protéines > >]
Duval, Valerie [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 > > >]
2010
Biomolecular NMR assignments
4
1
111-4
Yes (verified by ORBi)
International
1874-270X
Netherlands
[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.
http://hdl.handle.net/2268/14572
also: http://hdl.handle.net/2268/33916
10.1007/s12104-010-9219-8

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