The chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie

Abstract

Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, it<br />is induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagent<br />K(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperone<br />ability of modified system by UV-Vis and fluorescence spectroscopy and theoretical calculation methods.