Reva B A, Finkelstein A V
Institute of Mathematical Problems of Biology, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.
Protein Eng. 1996 May;9(5):399-411. doi: 10.1093/protein/9.5.399.
In a preceding paper we presented a novel approach to computation of 3-D folds of protein chains from their amino acid sequences. This approach is a physically correct generalization of the 'threading' methods. It is based on a self-consistent molecular field theory and on a physical theory of protein folding patterns, which make it possible to examine all the variety of 'potentially stable' folding patterns and all the variety of the chain conformations within each of them and to determine the thermodynamically stable structure. In this paper, we apply this approach to single out stable folding patterns and conformations for the chains of beta-sandwich proteins and show that the similarity of the calculated and observed structures is usually rather close.
在之前的一篇论文中，我们提出了一种从氨基酸序列计算蛋白质链三维折叠的新方法。这种方法是对“穿线法”的一种物理上正确的推广。它基于自洽分子场理论和蛋白质折叠模式的物理理论，这使得能够研究所有各种“潜在稳定”的折叠模式以及其中每一种模式内的所有各种链构象，并确定热力学稳定结构。在本文中，我们应用这种方法来挑选出β - 三明治蛋白质链的稳定折叠模式和构象，并表明计算结构与观察结构之间的相似性通常相当接近。
