Article
Thermal cycling aids folding of a recombinant human beta-casein with four extra N-terminal amino acid residues.
Archives of biochemistry and biophysics - 15 Nov 2000
Hu Y, Sood S M, Slattery C W
Abstract excerpt
Due to the limited secondary structure, it is believed that the caseins of milk, particularly the beta-caseins (beta-CN), may be in a mostly random-coil conformation or in various structures that result from random association of hydrophobic residues. However, the self-association of the human proteins with increasing temperature (T) and in the presence of Ca2+ is reproducible, implying that they normally fold...
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