Galzitskaya Oxana V, Bogatyreva Natalya S, Ivankov Dmitry N
Institute of Protein Research, Russian Academy of Sciences, Institutskaya Str. 4, Pushchino, Moscow Region 142290, Russia.
J Bioinform Comput Biol. 2008 Aug;6(4):667-80. doi: 10.1142/s0219720008003618.
We have demonstrated here that protein compactness, which we define as the ratio of the accessible surface area of a protein to that of the ideal sphere of the same volume, is one of the factors determining the mechanism of protein folding. Proteins with multi-state kinetics, on average, are more compact (compactness is 1.49+/-0.02 for proteins within the size range of 101-151 amino acid residues) than proteins with two-state kinetics (compactness is 1.59+/-0.03 for proteins within the same size range of 101-151 amino acid residues). We have shown that compactness for homologous proteins can explain both the difference in folding rates and the difference in folding mechanisms.
我们在此证明，蛋白质紧密性（我们将其定义为蛋白质可及表面积与相同体积理想球体可及表面积之比）是决定蛋白质折叠机制的因素之一。平均而言，具有多态动力学的蛋白质比具有两态动力学的蛋白质更紧密（对于101 - 151个氨基酸残基大小范围内的蛋白质，紧密性为1.49±0.02）（对于相同大小范围101 - 151个氨基酸残基的蛋白质，两态动力学蛋白质的紧密性为1.59±0.03）。我们已经表明，同源蛋白质的紧密性可以解释折叠速率的差异和折叠机制的差异。
