Solvent dependence of dimensions of unfolded protein chains.
The radii of gyration of unfolded apo-cytochrome C at pH 2.3 have been determined in three conditions: (i) 20 mM sodium phosphate buffer; (ii) 0.25 M NaCl; and (iii) 6.65 M GuHCl by small-angle X-ray scattering, and (iii) from translational diffusion coefficients measured by dynamic light scattering. The radius of gyration of the unfolded protein chain depends remarkably on the quality of the solvent, decreasing in the order 20 mM sodium phosphate greater than 6.65 M GuHCl greater than 0.25 M NaCl. The value of the radius of gyration in 0.25 M NaCl and also the value estimated for infinite ionic strength are close to the value predicted theoretically for the theta-point. This means that water in the absence of electrostatic interactions is a poor solvent for an unfolded protein while 6.65 M GuHCl is a better solvent.
Damaschun
G
G
Institute of Molecular Biology, Berlin-Buch, Germany.
Damaschun
H
H
Gast
K
K
Zirwer
D
D
Bychkova
V E
VE
D000818:Animals; D001059:Apoproteins / Q000737:chemistry*; D003574:Cytochrome c Group / Q000737:chemistry*; D045304:Cytochromes c; D008027:Light; D008433:Mathematics; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012542:Scattering, Radiation; D012997:Solvents; D014961:X-Ray Diffraction / Q000379:methods
D001059:Apoproteins; D003574:Cytochrome c Group; D011506:Proteins; D012997:Solvents; D045304:Cytochromes c