3P061 The circumventing mechanism of the folding of β-lactoglobulin(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

Abstract

Bovine β-lactoglobulin (βLG) has a folding intermediate with a non-native α-helical structure. Our previous study indicated that the moderate αhelical propensity of the wild-type sequence likely contributes to circumventing non-productive intermediates. In the present study, we analyzed the dynamics of the denatured βLG and performed high-pressure NMR measurements and H/D exchange pulse labeling experiments to obtain structural information of the intermediates. The results suggested that the three portions of the sequence, the C-terminal, the middle, and the N-terminal regions, sequentially attain individual native structures. Probably, the order of folding of these regions is programed in the βLG sequence to avoid non-native aggregations.