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Nanosecond time-resolved polarization spectroscopy a

机译：纳秒时间分辨偏振光谱法

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Abstract: The dynamic response of a protein to photoinitiation of folding can reveal new information about the early stages of secondary and tertiary structure formation, information beyond that obtainable from x-ray crystallography, NMR, and other steady state methods. The combined efforts of time- resolved studies using different experimental probes have already observed several events in the early stages of protein and peptide folding. However, in terms of the 'big folding picture', our understanding of protein folding is limited. Information on the folding mechanisms for a range of peptides and proteins is important to address the commonality of folding intermediates and pathways, but it is also useful to thoroughly understand the process of folding in at least one protein. To obtain such an understanding of one protein it is useful to employ a number of spectroscopic approaches We present here the results of time-resolved absorption, CD and MCD studies of the folding reactions of reduced cytochrome c after ligand photolysis of the CO adduct. We also discuss our results and the results of other studies on cytochrome c to demonstrate the advantage of using a number of different approaches for understanding protein folding. !36
机译：摘要：蛋白质对折叠光引发的动态响应可以揭示有关二级和三级结构形成早期的新信息，这些信息超出了通过X射线晶体学，NMR和其他稳态方法可获得的信息。使用不同的实验探针进行时间分辨研究的共同努力已经观察到蛋白质和肽折叠早期的一些事件。然而，就“大折叠图”而言，我们对蛋白质折叠的理解是有限的。关于多种肽和蛋白质的折叠机制的信息对于解决折叠中间体和途径的共通性很重要，但对于全面了解至少一种蛋白质的折叠过程也很有用。为了获得对一种蛋白质的这种理解，采用多种光谱方法是有用的。我们在此介绍了在CO加合物配体光解后还原的细胞色素c的折叠反应的时间分辨吸收，CD和MCD研究的结果。我们还将讨论我们的结果以及其他有关细胞色素c的研究结果，以证明使用多种不同方法来理解蛋白质折叠的优势。 ！36

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