THERMODYNAMIC AND KINETIC STUDIES OF PROTEIN STRUCTURE AND ENZYME MECHANISMS

在暴露于酸、pH时，猪胃蛋白酶原经历自我切割， 产生假胃蛋白酶，通过失去其前16个残基， 顺序 回到中性，产生不可逆构象 假胃蛋白酶变为新的球状形式，似乎与 到快速形成的瞬态中间体之前检测到的过程中， 完整胃蛋白酶原的折叠。 类似胃蛋白酶原，但不同于天然假 胃蛋白酶，这种中性pH形式的蛋白质可以可逆地解折叠， 折叠反应的机理，结构和 这种中性pH形式的假胃蛋白酶的稳定性和 胃蛋白酶原折叠机制中的前16个残基都在 调查

On exposure to acid, pH, swine pepsinogen undergoes self cleavage to produce psuedo pepsin, by the loss of the first 16 residues in its sequence. Returning to neutrality, produces an irreversible conformational change in psuedo pepsin to a new globular form, which seems to be identical to the rapidly formed transient intermediate previously detected during the folding of intact pepsinogen. Like pepsinogen, but unlike native psuedo pepsin, this neutral pH form of the protein can be reversibly unfolded by urea or high pH. The mechanism of the folding reaction, the structure and stability of this neutral pH form of psuedo pepsin and the role of the first 16 residues in the mechanism of folding of pepsinogen are all under investigation.