RELATIONSHIP OF STRUCTURE TO EFFECTIVENESS OF DENATURING AGENTS FOR PROTEINS
RELATIONSHIP OF STRUCTURE TO EFFECTIVENESS OF DENATURING AGENTS FOR PROTEINS
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DOI：
10.1021/bi00901a011
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发表时间：
1963-01-01
期刊：
影响因子：
2.9
通讯作者：
JENCKS, WP
中科院分区：
文献类型：
--
作者：
GORDON, JA;JENCKS, WP
测定了大量化合物对牛血清白蛋白旋光度的影响。旋光度的变化被解释为血清白蛋白变性的指示。所研究的化合物的有效性与它们作为氢供体或受体的预期氢键结合能力没有相关性，因此不支持它们的作用机制涉及与蛋白质形成简单的单官能氢键的假设。双官能氢键可以解释它们的有效性，但有必要假设不止一种类型的双官能氢键来解释所有活性化合物的作用。在血清白蛋白的情况下，观察到的影响不是由于溶液疏水性的增加，因为与变性剂的疏水性没有相关性或负相关性。更有限的研究与卵清蛋白，溶解度以及旋光度测量的基础上，证实了结论与牛血清白蛋白的氢键在变性中的作用，但表明，在卵清蛋白的情况下，有显着的贡献的疏水特性的化合物检查其变性的有效性。
The effect of a large number of compounds on the optical rotation of bovine serum albumin has been determined. The changes in optical rotation are interpreted as an indication of serum albumin denaturation. The effectiveness of the compounds examined shows no correlation with their expected hydrogen-bonding ability, as either hydrogen donors or acceptors, and thus provides no support for the hypothesis that their mechanism of action involves simple, monofunctional hydrogen bond formation with the protein. Bifunctional hydrogen bonding may explain their effectiveness, but it is necessary to postulate more than a single type of such bifunctional hydrogen bonding to explain the action of all active compounds. In the case of serum albumin, the observed effects are not due to an increase in the hydrophobic character of the solution, since there is either no correlation or a negative correlation with the hydrophobic character of the denaturing agents. More limited studies with ovalbumin, based on solubility as well as optical rotation measurements, confirm the conclusions reached with bovine serum albumin with respect to the role of hydrogen bonding in denaturation, but suggest that in the case of ovalbumin there is a significant contribution of the hydrophobic character of the compounds examined to their denaturing effectiveness.