An approximate treatment of long-range interactions in proteins
An approximate treatment of long-range interactions in proteins
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蛋白质长程相互作用的近似处理
DOI：
10.1021/j100531a013
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发表时间：
1977
期刊：
影响因子：
--
通讯作者：
H. Scheraga
中科院分区：
文献类型：
--
作者：
M. Pincus;H. Scheraga
本文提出了一种计算蛋白质残基间长程相互作用能的近似方法，该方法在临界距离以外是有效的。这种近似的结果在很大程度上减少了计算能量所需的计算机时间，与通常的程序相比，在相互作用的残留物中的所有原子对的相互作用。超过每个残基中方便的参考原子之间的临界距离，长程非键合（吸引）能可以近似为-By/（By）6，其中By是上述参考原子之间的距离，并且长程静电能可以被评估为每个残基上的正电荷和负电荷中心之间的库仑相互作用能。在这种近似方法中，残基之间的相互作用是根据残基的性质而不是每个残基的单个原子的性质来计算的。
An approximate method, valid beyond a critical distance, is presented for evaluating the long-ránge interaction energies betweenthe residues of a protein. This approximation results in large reductions in the computer time required toevaluate the energies, compared to the usual procedure of summing the interactions over all pairs of atoms in the interacting residues. Beyond a critical distance between convenient reference atoms in each residue, the long-range nonbonded (attractive) energy may be approximated by-By/(By) 6, whereBy is the distance between the above-mentioned reference atoms, and the long-range electrostatic energy may be evaluated as the Coulombic interaction energy between the centers of positive and negative charge on each residue. In thisapproximate procedure, the interactions between residues are computed in terms of properties of the residues instead of those of the individual atoms of each residue.