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首页> 外文期刊>Nature structural biology >COOPERATIVITY OF FOLDING OF THE APOMYOGLOBIN PH 4 INTERMEDIATE STUDIED BY GLYCINE AND PROLINE MUTATIONS
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COOPERATIVITY OF FOLDING OF THE APOMYOGLOBIN PH 4 INTERMEDIATE STUDIED BY GLYCINE AND PROLINE MUTATIONS

机译：甘氨酸和脯氨酸诱变合成的变形单核球蛋白PH 4中间体的折叠性

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摘要

The apomyoglobin pH 4 folding intermediate contains the A, G, and H helices of myoglobin. Helix destabilizing mutations in the A and G helices are used to test whether the pH 4 folding intermediate of apomyoglobin folds cooperatively. Single glycine or proline mutations destabilize the intermediate substantially, showing that intrinsic helix propensities are important for stability of the intermediate. The A and G helices interact to stabilize each other, as shown by the effect of mutations in the G helix on the unfolding of the A helix, which can be monitored by tryptophan fluorescence. Wild type and the most stable mutant unfold in a two-state reaction, as shown by superposition of the unfolding curves measured by two probes (far-UV circular dichroism and Trp fluorescence), while unfolding of the less stable mutants is more complex. Cooperativity and stability of folding are linked also when stabilizing anions (sulphate, perchlorate) are used to adjust stability. [References: 24]
机译：磷酸肌红蛋白pH 4折叠中间体包含肌红蛋白的A，G和H螺旋。 A和G螺旋中的螺旋破坏稳定突变用于测试磷肌红蛋白的pH 4折叠中间体是否协同折叠。单个甘氨酸或脯氨酸突变会大大破坏中间体的稳定性，表明内在的螺旋倾向对于中间体的稳定性很重要。 A和G螺旋相互作用以彼此稳定，如G螺旋中的突变对A螺旋的展开所产生的影响所示，这可以通过色氨酸荧光进行监测。野生型和最稳定的突变体在两个状态的反应中展开，如通过两个探针（远紫外圆二色性和Trp荧光）测量的展开曲线的叠加所示，而不稳定程度较低的突变体的展开则更为复杂。当使用稳定阴离子（硫酸根，高氯酸根）来调节稳定性时，折叠的协同性和稳定性也联系在一起。 [参考：24]

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