Kataoka M, Goto Y
Department of Earth and Space Science, Osaka University, Japan.
Fold Des. 1996;1(5):R107-14. doi: 10.1016/S1359-0278(96)00047-8.
Protein folding is a reaction in which an extended polypeptide chain acquires maximal packing through formation of secondary and tertiary structures. Compactness and shape are, therefore, critical properties characterizing the process of protein folding. Because the stability of the native state is determined by the subtle free energy balance between the native and denatured states, the characterization of the denatured state is also essential to understand the conformational stability of the native state. We show that solution X-ray scattering is the best technique available today to address these problems. Although the structural resolution of the unfolded or compact denatured states elucidated from solution X-ray scattering is low, it provides a variety of information complementary to that obtained by NMR or X-ray crystallography.
蛋白质折叠是一个反应过程，在此过程中，一条伸展的多肽链通过形成二级和三级结构获得最大程度的堆积。因此，紧密性和形状是表征蛋白质折叠过程的关键特性。由于天然态的稳定性由天然态和变性态之间微妙的自由能平衡决定，所以变性态的表征对于理解天然态的构象稳定性也至关重要。我们表明，溶液X射线散射是当今解决这些问题的最佳可用技术。尽管从溶液X射线散射阐明的未折叠或紧密变性态的结构分辨率较低，但它提供了与通过核磁共振（NMR）或X射线晶体学获得的信息互补的各种信息。
