1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozym
 

1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme.

Related Articles 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme.

Biochemistry. 1990 Aug 7;29(31):7201-14

Authors: Redfield C, Dobson CM

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.

PMID: 2207098 [PubMed - indexed for MEDLINE]



Source: PubMed