Finkelstein A V, Reva B A
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.
Protein Eng. 1996 May;9(5):387-97. doi: 10.1093/protein/9.5.387.
We present a general approach to the prediction of 3-D folds of protein chains from their amino acid sequences. The approach is based on the use of the self-consistent molecular field theory for long-range interactions, the use of 1-D statistical mechanics for short-range interactions and on the discovery that there is and should only be a relatively small discrete set of folding patterns. This makes it possible to examine the full variety of 'potentially stable' folds and to determine the thermodynamically stable structure. In this paper, we give the general theoretical background of the approach. The encouraging results of the application of this approach to beta-domains are described in another paper.
我们提出了一种从蛋白质链的氨基酸序列预测其三维折叠结构的通用方法。该方法基于使用自洽分子场理论处理长程相互作用、使用一维统计力学处理短程相互作用，以及发现存在且应该只存在相对较小的一组离散折叠模式。这使得研究所有“潜在稳定”折叠的多样性并确定热力学稳定结构成为可能。在本文中，我们给出了该方法的一般理论背景。此方法应用于β结构域的令人鼓舞的结果在另一篇论文中进行了描述。
