Aszódi A, Taylor W R
Laboratory of Mathematical Biology, National Institute for Medical Research, Mill Hill, London, UK.
Protein Eng. 1994 May;7(5):633-44. doi: 10.1093/protein/7.5.633.
Model polypeptide chains were folded into 3-D compact conformations using distance geometry techniques. Interresidue distances were predicted from the hydrophobicity of the monomers and were refined by repeated projections into lower-dimensional spaces. Main-chain hydrogen bond networks were constructed and propagated through the structure by adjusting local conformations to comply with ideal distance constraints around hydrogen bonds. The resulting folds were compact globules with distinct hydrophobic cores and contained secondary structure elements like real protein molecules. Apart from similarity in appearance, several properties of the model chains were also very close to those of native folded polypeptides. The method in its present form can serve as a starting point for the development of a novel structure prediction algorithm.
使用距离几何技术将模型多肽链折叠成三维紧密构象。根据单体的疏水性预测残基间距离，并通过反复投影到低维空间进行优化。构建主链氢键网络，并通过调整局部构象使其符合氢键周围的理想距离约束，从而在整个结构中传播。生成的折叠结构是具有明显疏水核心的紧密球体，并包含如真实蛋白质分子般的二级结构元件。除了外观相似外，模型链的几个性质也与天然折叠多肽非常接近。目前形式的该方法可作为开发新型结构预测算法的起点。
