Abstract
Hen egg-white lysozyme, the most widely studied of the chicken-type lysozymes, is an enzyme containing 129 amino acid residues, and it has been prepared in at least seven crystalline forms. The mechanism of action of lysozyme in cleaving the muco-polysaccharides of certain bacterial cell walls is now well understood, largely as a result of crystallographic investigations; see Imoto et al. (5) for a review. While crystallographic work continues in several laboratories, some aspects of the way lysozyme works in solution have been reexamined or clarified, in particular by high resolution NMR work (3), quantum-chemical calculations (12), and molecular dynamics calculations (9).
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Mason, S.A., Bentley, G.A., McIntyre, G.J. (1984). Deuterium Exchange in Lysozyme at 1.4-Å Resolution. In: Schoenborn, B.P. (eds) Neutrons in Biology. Basic Life Sciences, vol 27. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0375-4_19
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DOI: https://doi.org/10.1007/978-1-4899-0375-4_19
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