ON THE PREDICTION OF PROTEIN-STRUCTURE - THE SIGNIFICANCE OF THE ROOT-MEAN-SQUARE DEVIATION
ON THE PREDICTION OF PROTEIN-STRUCTURE - THE SIGNIFICANCE OF THE ROOT-MEAN-SQUARE DEVIATION
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DOI：
10.1016/0022-2836(80)90289-2
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发表时间：
1980-01-01
影响因子：
5.6
通讯作者：
STERNBERG, MJE
中科院分区：
文献类型：
--
作者：
COHEN, FE;STERNBERG, MJE
预测的蛋白质结构中原子位置与天然坐标的均方根偏差通常被报告为指示折叠模拟的成功。本研究报告了一种方法，并量化的意义，获得一个特定的均方根偏差折叠不同分子量的蛋白质时。对于12种蛋白质中的每一种，通过计算高效的算法生成一系列随机紧凑结构，并将这些结构与天然结构进行比较。的平均均方根偏差是成比例的残基的数量和这种相关性是由一个数学模型来解释。从偏差值的分布，不同的折叠研究的成功进行评估方面可能的紧凑的球状褶皱的数量。
The root-mean-square deviation of the atomic positions in a predicted protein structure from the native co-ordinates is commonly reported to indicate the success of the folding simulation. This study reports a method and quantifies the significance of obtaining a specific root-mean-square deviation when folding proteins of different MW. For each of 12 proteins a series of random compact structures is generated by a computationally efficient algorithm and these structures are compared to the native. The average root-mean-square deviation is proportional to the number of residues and this correlation is explained by a mathematical model. From the distribution of the values of the deviations, the success of different folding studies is assessed in terms of the number of possible compact globular folds.