[NMR study of beta-structures in the compact non-native states of globular proteins].
By the high resolution NMR method was made comparative research of carboanhydrase B, alpha-lactalbumin and apomyoglobin in a molten globular state. It is shown that though in an observed spectra the typical signals at 5.7-5 ppm, responding to the signals of alpha-CH protons of the beta-structure, method of spin diffusion proves that after all is taking place in carboanhydrase B and alpha-lactalbumin, that corresponds with the data of CD.
Kutyshenko
A V
AV
Kutyshenko
V P
VP
Kivaeva
L S
LS
D000818:Animals; D001059:Apoproteins / Q000737:chemistry*; D002256:Carbonic Anhydrases / Q000737:chemistry*; D002417:Cattle; D006736:Horses; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D012996:Solutions
D001059:Apoproteins; D009211:Myoglobin; D012996:Solutions; C010857:apomyoglobin; D007768:Lactalbumin; D002256:Carbonic Anhydrases