THERMODYNAMIC AND KINETIC STUDIES OF PROTEIN STRUCTURE AND ENZYME MECHANISMS

蛋白质结构和酶机制的热力学和动力学研究

• 批准号: 4689040
• 负责人: P MCPHIE
• 金额: --
• 依托单位: NAT INST OF ARTHRITIS, DIABETES, DIGESTIVE & KIDNEY DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/4689040
• 关键词: chelation therapy; chemical structure function; circular dichroism; conformation; drug design /synthesis /production; enzyme induction /repression; enzyme structure; pepsin; pepsinogens; stop flow technique; ultraviolet spectrometry; zymogens

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.

猪胃蛋白酶原暴露于酸、pH下，发生自裂解