The core of apomyoglobin E-form folds at the diffusion limit
The core of apomyoglobin E-form folds at the diffusion limit
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DOI：
10.1038/nsb0598-363
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发表时间：
1998-05-01
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影响因子：
--
通讯作者：
Dyer, RB
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文献类型：
--
作者：
Gilmanshin, R;Callender, RH;Dyer, RB
用红外光谱和荧光光谱对脱脂肌红蛋白的E-型进行了表征，显示出一个紧密的核心，具有天然的接触，最可能由脱脂肌红蛋白的A、G和H螺旋的15-20个残基组成。快速温度跳跃、时间分辨红外测量表明，在46摄氏度下，核心在96亩S范围内形成，接近形成环的扩散极限。值得注意的是，E-型的折叠路径使得有限数量的类自然接触的形成不是速率限制的，或者接触形成的时间尺度与扩散控制环形成的预期时间尺度相同。
The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 mu s at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation.