A small-angle neutron scattering measurement was done for a lysozyme sample in aqueous solutions with different D>O/H,O ratios. Structure parameters such as R,,, a and p and the scattering functions such as I,(Q), I,(Q) and I,,(Q) were obtained.
Influence of pH on the dielectric properties of egg-white lysozyme in aqueous solution
β Scribed by A.A. Laogun
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 420 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0167-7322
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The surface properties of aqueous egg albumen protein solutions (0.1 g litre Γ1 ) were studied at pH values of 4.8, 7.0, 9.2 and 10.7 and related to foaming behaviour such as bubble size distribution, overrun and drainage. By measurements far from equilibrium of dynamic steady state surface dilation
In the present study, the equilibrium and kinetic analysis on the folding of hen egg lysozyme in the aqueous-glycerol solutions have been reported by means of fluorescence and circular dichroism spectra. Addition of glycerol increases the stability of lysozyme on the guanidine-induced denaturation,
Preferential interactions between proteins and metals play an important role in a great number of physiological and biochemical processes. With these premises, the inΓuence of LiCl on the conformation and function of lysozyme has been the main object of our studies. Viscometric, densimetric, solubil
A partly folded state of hen egg-white lysozyme has been characterized in 50% DMSO. Low concentrations of DMSO (F10%) have little effect on the overall folded conformation of lysozyme as seen from 1 H NMR chemical shift dispersion. At increasing DMSO concentrations (G10%) a cooperative transition of