Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1007/s12104-010-9219-8

Type

Journal article

Journal

Biomol NMR Assign

Publication Date

04/2010

Volume

4

Pages

111 - 114

Keywords

Bacteriophage lambda, Carbon Isotopes, Escherichia coli, Hydrogen, Muramidase, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Viral Proteins