Adams B, Burgess R J, Pain R H
Eur J Biochem. 1985 Nov 4;152(3):715-20. doi: 10.1111/j.1432-1033.1985.tb09252.x.
Analysis of the reversible unfolding of yeast phosphoglycerate kinase leads to the conclusion that the two lobes are capable of folding independently, consistent with the presence of intermediates on the folding pathway with a single domain folded. The domains have different free energies of stabilisation. Immunological cross-reactivity, circular dichroism and thiol reactivity provide evidence for cyanogen bromide peptide 1-173, which comprises five-sixths of the N-terminal domain, containing sufficient information to refold into a native-like structure which dimerises.
对酵母磷酸甘油酸激酶可逆去折叠的分析得出结论，即两个叶能够独立折叠，这与折叠途径中存在具有单个折叠结构域的中间体一致。这些结构域具有不同的稳定自由能。免疫交叉反应性、圆二色性和硫醇反应性为溴化氰肽1 - 173提供了证据，该肽包含N端结构域的六分之五，含有足够的信息重新折叠成二聚化的类似天然的结构。
