Raghunathan G, Jernigan R L
Molecular Structure Section, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5677, USA.
Protein Sci. 1997 Oct;6(10):2072-83. doi: 10.1002/pro.5560061003.
A simple model of sphere packing has been investigated as an ideal model for long-range interactions for the packing of non-bonded residues in protein structures. By superposing all residues, the geometry of packing around a central residue is investigated. It is found that all residues conform almost perfectly to this lattice model for sphere packing when a radius of 6.5 A is used to define non-bonded (virtual) interacting residues. Side-chain positions with respect to sequential backbone segments are relatively regular as well. This lattice can readily be used in conformation simulations to reduce the conformational space.
作为蛋白质结构中非键合残基堆积的长程相互作用的理想模型,人们研究了一种简单的球体堆积模型。通过叠加所有残基,研究了中心残基周围的堆积几何结构。结果发现,当使用6.5埃的半径来定义非键合(虚拟)相互作用残基时,所有残基几乎完全符合这种球体堆积的晶格模型。侧链相对于连续主链片段的位置也相对规则。这种晶格可很容易地用于构象模拟,以减少构象空间。