Ikeguchi Masamichi
Department of Bioinformatics, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, Japan.
Biomolecules. 2014 Feb 13;4(1):202-16. doi: 10.3390/biom4010202.
In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using the non-native helix formation during the folding of β-lactoglobulin as a prominent example. Although β-lactoglobulin is a predominantly β-sheet protein, it has been shown to form non-native helices during the early stage of folding. The location of non-native helices, their stabilization mechanism, and their role in the folding reaction are discussed.
在理想蛋白质中，只有天然相互作用在类似漏斗状的平滑能量景观中逐步稳定下来。然而，在实际蛋白质中，非天然结构的瞬时形成却经常被观察到。在本综述中，以β-乳球蛋白折叠过程中形成非天然螺旋为例，描述了非天然结构的瞬时形成。尽管β-乳球蛋白主要是一种β-折叠蛋白，但已证明它在折叠早期会形成非天然螺旋。本文讨论了非天然螺旋的位置、其稳定机制以及它们在折叠反应中的作用。
