Barrick Doug
T C Department of Biophysics, The Johns Hopkins University, 3400 N Charles St, Baltimore, MD 21218, USA.
Phys Biol. 2009 Feb 10;6(1):015001. doi: 10.1088/1478-3975/6/1/015001.
Small proteins with globular structures often fold by simple all-or-none mechanisms, both in an equilibrium and a kinetic sense, despite the very large number of partly folded conformations available. This type of 'two-state' folding will be discussed in terms of experimental tests, underlying molecular mechanisms, and limits to two-state behavior. Factors that appear to be important for two-state folding include topology (sequence distance of contacts in the native structure), molecular cooperativity and local energy distribution. Because their local stability distributions and cooperativities can be dissected and analyzed separately from topological features, recent studies of the folding of symmetric proteins will be discussed as a means to better understand the origins of two-state folding.
具有球状结构的小蛋白质通常通过简单的全或无机制进行折叠，无论是在平衡还是动力学意义上，尽管存在大量部分折叠的构象。这种“两态”折叠将从实验测试、潜在分子机制以及两态行为的局限性等方面进行讨论。对于两态折叠似乎很重要的因素包括拓扑结构（天然结构中接触的序列距离）、分子协同性和局部能量分布。由于它们的局部稳定性分布和协同性可以与拓扑特征分开剖析和分析，因此将讨论对称蛋白质折叠的最新研究，以此作为更好地理解两态折叠起源的一种手段。
