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

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... ee 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. 3P062 アポミオグロビンのドメインスワッピングとフォールディン グの競合:分子シミュレーション解析 Monomer folding versus dimer domain-swapping in apomyoglobin studied by molecular simulations