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Energetics of denaturation and m values of staphylococcal nuclease mutants.

机译：葡萄球菌核酸酶突变体的变性和m值的能量学。

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摘要

In a continuation of an earlier study [Carra, J., Anderson, E., & Privalov, P. (1994) Biochemistry 33, 10842-10850], we used differential scanning calorimetry to measure the enthalpy and heat capacity changes of denaturation for 11 mutant forms of staphylococcal nuclease, including the triple mutant [V66L+G88V+G79S]. Several mutant proteins with m- characteristics of guanidinium chloride denaturation were found to denature via a three-state mechanism with increasing temperature. Enthalpy changes for the transitions from the native to intermediate and from the intermediate to denatured states were determined. In the case of the triple mutant, the enthalpy of the second endothermic transition is greater than that of the first. Observation of this second transition provides an explanation for the previously reported large changes in the delta H denaturation for the triple mutant versus wild-type nuclease. The sequence specificity of structure in the intermediate state is discussed with relevance to m values of guanidinium chloride denaturation. The enthalpic level of the intermediate state depends upon the amino acid sequence, suggesting that stabilizing mutations can increase the extent or cohesion of structure present in the intermediate.
机译：在先前研究的延续中[Carra，J.，Anderson，E.，＆Privalov，P.（1994）Biochemistry 33，10842-10850]，我们使用差示扫描量热法测量了变性的焓和热容变化。金黄色葡萄球菌核酸酶的11种突变形式，包括三突变体[V66L + G88V + G79S]。发现具有m-特征的氯化胍变性的一些突变蛋白通过三态机制随着温度升高而变性。确定了从天然状态到中间状态以及从中间状态到变性状态的转变的焓变。在三重突变体的情况下，第二个吸热转变的焓大于第一个。观察到该第二过渡为先前报道的三突变体相对于野生型核酸酶的ΔH变性的大变化提供了解释。结合氯化胍变性的m值讨论了处于中间状态的结构的序列特异性。中间体状态的焓水平取决于氨基酸序列，表明稳定的突变可以增加中间体中存在的结构的程度或内聚力。

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