Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states.

doi:10.1007/s10858-005-2063-y

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Article

Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states.

Journal of biomolecular NMR - 1 Oct 2005

Schlörb Christian, Ackermann Katrin, Richter Christian, Wirmer Julia, Schwalbe Harald

Abstract excerpt

A new protocol is described for the isotope (15N and 13C,15N) enrichment of hen egg white lysozyme. Hen egg white lysozyme and an all-Ala-mutant of this protein have been expressed in E. coli. They formed inclusion bodies from which mg quantities of the proteins were purified and prepared for NMR spectroscopic investigations. 1H,13C and 15N main chain resonances of disulfide reduced and S-methylated lysozyme were...

Topics

Animals
Carbon Isotopes
Chickens
Escherichia coli
Hydrophobic and Hydrophilic Interactions
Indoles
Methylation
Muramidase
Mutation
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Recombinant Proteins
Tryptophan

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Identifiers

PMID: 16258828
DOI: 10.1007/s10858-005-2063-y

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