The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse.
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机译：apglooglobin的快速重折叠动力学，然后是在15 ns到0.5 ms的时间尺度上体外的新的温度跳跃荧光技术。该仪器在标准水性缓冲液中一次扫描即可测量蛋白质折叠历史。观察到折叠到紧凑状态的最早步骤，并在20微米以下完成。对突变体进行的实验以及对稳态CD和荧光光谱的考虑表明，观察到的微秒相监视着A x（H x G）螺旋亚基的组装。在不同粘度下的测量结果表明，即使在低粘度下也具有扩散行为，这与初始崩解过程中溶剂暴露的蛋白质的运动一致。
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