Circular dichroic study of conformational changes in ovalbumin.
By simulation of the circular dichroic spectra (Greenfield and Fasman (1969] and using reference spectra of Chen et al. (1974), native ovalbumin was estimated to contain 33% alpha-helix, 5% beta-structure, and 62% random coil. Ovalbumin resisted conformational changes in solutions of urea and of SDS. However, guanidine induced transition, starting at about 2 M and completing at about 4.5 M. At concentrations exceeding 4.5 M guanidine, ovalbumin existed as 6-7% alpha-helical, 12-13% beta-structure, and 80-81% random coil. Ovalbumin after denaturation in 6 M guanidine or in 8 M urea (incubated at 4 degrees C for 24 hr) did not recover the native conformation but acquired a new conformation in each case, with a somewhat destabilized helical structure.
Batra
P P
PP
Department of Biochemistry, Wright State University, Dayton, Ohio 45435.
Sasa
K
K
Ueki
T
T
Takeda
K
K
D002942:Circular Dichroism; D007700:Kinetics; D010047:Ovalbumin / Q000378:metabolism; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D014508:Urea / Q000494:pharmacology
D012967:Sodium Dodecyl Sulfate; D014508:Urea; D010047:Ovalbumin