[Spin diffusion in globular proteins: alpha-lactalbumin].
The structural properties of globular proteins analyzed by two different methods: high-resolution NMR and circular dichroism were compared. We established that the spin diffusion method shows changes in the secondary structure during the unfolding of the alpha-lactalbumin molten globule by urea. It was shown that the spin diffusion method is extremely effective in studies of interactions of water and denaturant molecules with the protein both in the native and the molten globule states.
Kutyshenko
V P
VP
Prokhorov
D A
DA
Khristoforov
V S
VS
D006147:Guanine / Q000737:chemistry; D006801:Humans; D007202:Indicators and Reagents; D007768:Lactalbumin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011489:Protein Denaturation; D014508:Urea / Q000737:chemistry; D014867:Water / Q000737:chemistry
D007202:Indicators and Reagents; D014867:Water; D006147:Guanine; D014508:Urea; D007768:Lactalbumin