Molecular dimensions and their distributions in early folding intermediates
Molecular dimensions and their distributions in early folding intermediates
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DOI：
10.1016/j.sbi.2006.01.007
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发表时间：
2006-02-01
影响因子：
6.8
通讯作者：
Matthews, CR
中科院分区：
文献类型：
--
作者：
Bilsel, O;Matthews, CR
超快混合技术与同步加速器上的明亮X射线源和复杂的荧光方法相结合，可以对折叠早期阶段出现的未折叠蛋白质和瞬时中间体的尺寸进行定量分析。时间分辨的福斯特共振能量转移和小角度X射线散射技术，这是敏感的距离分布，也可以阐明的过程，否则掩盖在一个单一的整体平均光学性能的测量的性质。这两种方法最近被应用于蛋白质折叠问题。特别是，在表征未折叠状态的尺寸方面取得了进展，并在折叠反应开始时区分未折叠状态的无障碍和障碍限制的崩溃。
The integration of ultrafast mixing technology with bright X-ray sources at synchrotrons and with sophisticated fluorescence methods is yielding quantitative insights into the dimensions of unfolded proteins and transient intermediates that appear during the earliest stages of folding. Time-resolved Forster resonance energy transfer and small-angle X-ray scattering techniques, which are sensitive to the distributions of distances, can also elucidate the nature of processes otherwise obscured in measurements of a single ensemble-averaged optical property. These two approaches have recently been applied to the protein folding problem. In particular, progress has been made in characterizing the dimensions of unfolded states, and discriminating between barrierless and barrier-limited collapse of the unfolded state at the beginning of the folding reaction.