Lobanov M Iu, Bogatyreva N S, Galzitskaia O V
Mol Biol (Mosk). 2008 Jul-Aug;42(4):701-6.
Search and study of the general principles that govern kinetics and thermodynamics of protein folding generate a new insight into the factors controlling this process. Statistical analysis of radii of gyration for 3769 protein structures from four general structural classes (all-alpha, all-beta, alpha/beta, alpha + beta) demonstrates that each class of proteins has its own class-specific radius of gyration, which determines compactness of protein structures: alpha-proteins have the largest radius of gyration. This indicates that they are less tightly packed than beta- and alpha + beta-proteins. Finally, alpha/beta-proteins are the most tightly packed proteins with the least radius of gyration. It should be underlined that radius of gyration normalized on the radius of gyration of ball with the same volume, is independent of the length in comparison with such parameters as compactness and number of contacts per residue.
对支配蛋白质折叠动力学和热力学的一般原理进行搜索和研究，能让我们对控制这一过程的因素有新的认识。对来自四种一般结构类型（全α、全β、α/β、α + β）的3769个蛋白质结构的回转半径进行统计分析表明，每一类蛋白质都有其特定类别的回转半径，这决定了蛋白质结构的紧凑程度：α蛋白质的回转半径最大。这表明它们的堆积不如β蛋白质和α + β蛋白质紧密。最后，α/β蛋白质是堆积最紧密、回转半径最小的蛋白质。需要强调的是，与紧凑性和每个残基的接触数等参数相比，用相同体积球体的回转半径进行归一化后的回转半径与长度无关。
