1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme.
Complete main-chain (NH and alpha CH) 1H NMR assignments are reported for the 130 residues of human lysozyme, along with extensive assignments for side-chain protons. Analysis of 2-D NOESY experiments shows that the regions of secondary structure for human lysozyme in solution are essentially identical with those found previously in a similar study of hen lysozyme and are in close accord with the structure of the protein reported previously from X-ray diffraction studies in the crystalline state. Comparison of the chemical shifts, spin-spin coupling constants, and hydrogen exchange behavior are also consistent with closely similar structures for the two proteins in solution. In a number of cases specific differences in the NMR parameters between hen and human lysozymes can be correlated with specific differences observed in the crystal structures.
Redfield
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Oxford Centre for Molecular Sciences, University of Oxford, England.
Dobson
C M
CM
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D013045:Species Specificity
D009113:Muramidase