FOLDING OF YEAST CYTOCHROME C

酵母细胞色素 C 的折叠

• 批准号: 6120973
• 负责人: WILLIAM A MCGEE
• 金额: $ 0.74万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6120973
• 关键词: biological products; biomaterials; biomedical resource; enzymes; nuclear magnetic resonance spectroscopy; proteins

In order to understand the mechanism of the interaction between chymotrypsin and its inhibitor - OMTKY3, it is necessary to relate the biochemical behavior of the mutants of OMTKY3 to their structural properties. pH titration by NMR can provide such information. By means of pH titration, we can obtain the pKa value of different amino acid residues. By comparison of these pKa values,, those of wild type and those of other mutants, we can obtain important structural information for OMTKY3 and arrive at a further understanding of its inhibitory action on chymotrypsin.

为了了解它们之间相互作用的机制， 胰凝乳蛋白酶及其抑制剂-OMTKY 3，有必要将 OMTKY 3突变体的生化行为对其结构的影响 特性. 通过NMR的pH滴定可以提供这样的信息。 通过 通过pH滴定法，可以得到不同氨基的pKa值 酸残留物。 通过比较这些pKa值， 和其他突变体的基因组，我们可以获得重要的结构 OMTKY 3的信息，并进一步了解其 对胰凝乳蛋白酶抑制作用。