Article
The effect of conserved residue charge reversal on the folding of recombinant non-phosphorylated human beta-casein.
Archives of biochemistry and biophysics - 15 Nov 2003
Bu Hongyin, Sood Satish M, Slattery Charles W
Abstract excerpt
A short stretch of 13 amino acids in the central portion of human beta-casein contains four positively charged conserved residues, three Lys and one Arg. We changed these individually to Glu, reversing their charge, and compared the resulting recombinant proteins to the wild-type recombinant, monitoring thermal aggregation with turbidity as well as using the fluorescence of the intrinsic Trp, of hydrophobically...
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