COMPACTNESS DETERMINES PROTEIN FOLDING TYPE
COMPACTNESS DETERMINES PROTEIN FOLDING TYPE
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DOI：
10.1142/s0219720008003618
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发表时间：
2008-08-01
影响因子：
1
通讯作者：
Ivankov, Dmitry N.
中科院分区：
文献类型：
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作者：
Galzitskaya, Oxana V.;Bogatyreva, Natalya S.;Ivankov, Dmitry N.
我们在这里已经证明了蛋白质的致密性，这是我们所描述的。Ne是蛋白质的可达表面积与相同体积的理想球体的表面积之比，是决定蛋白质折叠机制的因素之一。平均而言，多态动力学的蛋白质比双态动力学的蛋白质更致密(101-151个氨基酸残基大小范围内的蛋白质紧凑度为1.49+/-0.02)(101-151个氨基酸残基大小相同的蛋白质紧密度为1.59+/-0.03)。我们已经证明，同源蛋白质的致密性可以解释折叠速度的差异和折叠机制的差异。
We have demonstrated here that protein compactness, which we de. ne 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 101-151amino 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.