作者: Leonard F. Liebes , Robert Zand , William D. Phillips
DOI: 10.1016/0005-2795(75)90311-6
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摘要: Abstract Bovine myelin basic protein has been investigated with regard to its solution behavior, circular dichroism and 220 MHz PMR spectral properties. At pH 4.8 γ/2 = 0.1 acetate buffer, light scattering yielded a Mr of 17 700 virial coefficient 1.0·10−4 mol·ml/g2. Above 7.0 the was found aggregate higher mol. wt species. Sedimentation experiments at s°20,w 1.27 S 1.46 0.35. The diffusion determined from ultracentrifugal 7.25·10−7 cm2/s value ƒ/ƒ 0 0.35 1.64, corresponding an axial ratio 11 1. radius gyration calculated as 4.28 nm root mean square end distance 10.5 nm. 9.0, 0.1, 1.71 D°20,w estimated 7.4·10−7 cm2/s. behavior 9.0 reverted when readjusted. E1cm1% 5.64 276.4 225 196 Titration trifluoroethanol elicited three distinct regions conformational stability having increasing helical content mol fraction increased. results present study have permitted some comparison analogous properties membrane cytochrome c.