sup 1 H NMR studies of human lysozyme: Spectral assignment and comparison with hen lysozyme

Journal Article · Tue Aug 07 00:00:00 EDT 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00483a007· OSTI ID:5935306

Redfield, C; Dobson, C M ^[1]

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1. Univ. of Oxford (England)

Complete main-chain (NH and {alpha}CH){sup 1}H 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.

• OSTI ID: 5935306
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:31; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
AMINO ACID SEQUENCE
ANIMALS
BARYONS
BIRDS
CHEMICAL SHIFT
CHICKENS
COHERENT SCATTERING
DIFFRACTION
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
FOWL
GLYCOSYL HYDROLASES
HADRONS
HYDROLASES
LYSOZYME
MAGNETIC RESONANCE
MAMMALS
MAN
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
O-GLYCOSYL HYDROLASES
OVERHAUSER EFFECT
PRIMATES
PROTONS
RESONANCE
SCATTERING
VERTEBRATES
X-RAY DIFFRACTION