Article (Scientific journals)
Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Di Paolo, Alexandre; Duval, Valerie; Matagne, André et al.
2010In Biomolecular NMR Assignments, 4 (1), p. 111-4
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Keywords :
Backbone resonance assignments; lysozyme; protein folding
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Di Paolo, Alexandre ;  Université de Liège - ULiège > Sciences de la Vie > Enzymologie et Repliement des Protéine, Centre d'ingénierie des protéines
Duval, Valerie;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Matagne, André  ;  Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines
Redfield, Christina;  University of Oxford > Department of Biochemistry
Language :
English
Title :
Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Publication date :
2010
Journal title :
Biomolecular NMR Assignments
ISSN :
1874-2718
eISSN :
1874-270X
Publisher :
Springer, Germany
Volume :
4
Issue :
1
Pages :
111-4
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 05 May 2010

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