3P066 Kinetic properties of pH-induced and salt-induced intermediates of horse apomyoglobin(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
3P066 ウマアポミオグロビンのpH4中間体と塩による中間体の速度論的性質(01C. 蛋白質:物性,ポスター,第52回日本生物物理学会年会(2014年度))

Yukiko Abe, Takuya Mizukami, Kosuke Maki
2014 Seibutsu Butsuri  
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
more » ... 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
doi:10.2142/biophys.54.s259_6 fatcat:x23mj6f3ofc65iukhvf62njkhi