Molecular hinges in protein folding: the urea-denatured state of apomyoglobin.
Molecular hinges in protein folding: the urea-denatured state of apomyoglobin.
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DOI：
10.1021/bi020381o
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发表时间：
2002-09
期刊：
影响因子：
2.9
通讯作者：
S. Schwarzinger;P. Wright;H. Dyson
中科院分区：
文献类型：
--
作者：
S. Schwarzinger;P. Wright;H. Dyson
在pH 2.3的8 M尿素中未折叠的脱辅基肌红蛋白显示具有不同骨架迁移率的不同区域，如通过NMR弛豫监测的。骨架迁移率的这些变化可以与序列中氨基酸的固有性质相关。与平均值相比，小氨基酸如甘氨酸和丙氨酸的簇显示出增加的主链移动性。相比之下，在脲变性剂中持续存在的局部疏水相互作用在皮秒至纳秒的时间尺度上引起主链运动的一些限制。从apoMb在尿素中的行为推导出的模型仅依赖于局部氨基酸序列的最基本性质，从而为折叠的起始提供了一个可行的范例。
Unfolded apomyoglobin in 8 M urea at pH 2.3 displays distinct regions with different backbone mobility, as monitored by NMR relaxation. These variations in backbone mobility can be correlated with intrinsic properties of the amino acids in the sequence. Clusters of small amino acids such as glycine and alanine show increased backbone mobility compared to the average. In contrast, local hydrophobic interactions that persist in urea denaturant cause some restriction of backbone motions on a picosecond to nanosecond time scale. The model derived from the behavior of apoMb in urea depends only on the most fundamental properties of the local amino acid sequence, and thus provides a feasible paradigm for the initiation of folding.