SELF RECOGNITION IN GLOBULAR PROTEINS

描述：蛋白质的三维结构是一个复杂的， 精巧的分子表意文字，包括 成千上万（通常是数万或数十万）的原子。 每种蛋白质都有 只有一种天然构象，而且，我们想知道它是什么，因为，对于一个 蛋白质分子，功能遵循形式。 也就是说，蛋白质的生物学特性 作用是其构象的结果。 通用分子文法 指定蛋白质构象。 这一论断是基于一个告诉 安芬森实验 虽然实验证明 生物化学家认为，这样的语法必须存在， 这是一个足以预测蛋白质构象仍然缺乏;这是 蛋白质折叠问题 蛋白质折叠问题已经成为一个重大的科学问题 这个世纪的挑战。 这个问题的解决方案对一个 了解天然存在的蛋白质及其故意 工程对应物。 罗斯博士的主要目标是阐明 控制蛋白质折叠的立体化学密码，并用它来制定一个 实用折叠算法 为此，他正在开发一种算法， LINUS，仅从其氨基酸序列预测蛋白质的折叠。 LINUS是Local Independently Nucleated Units of Structure的缩写。 该过程在不连续的阶段中沿着折叠层次上升， 每一步都伴随着结构的增加。 链表示 通过简化的几何形状和褶皱， 能量函数 目前的结果令人鼓舞。

DESCRIPTION: The three-dimensional structure of a protein is a complex, exquisitely fashioned molecular ideogram, involving interactions among thousands (often tens or hundreds of thousands) of atoms. Each protein has only one native conformation, and, we want to know what it is because, for a protein molecule, function follows form. That is, a protein's biological role is a consequence of its conformation. A universal molecular grammar specifies protein conformation. This assertion is based on a telling experiment, the Anfinsen experiment. While the experiment convinced biochemists that such a grammar must exist, a level of understanding sufficient to predict protein conformation is still lacking; and that is the protein folding problem. The protein folding problem has emerged as one of the great scientific challenges of this century. The solution to this problem is critical to an understanding of the naturally occurring proteins and their deliberately engineered counterparts. Dr. Rose's principal goal is to elucidate the stereochemical code that governs protein folding and use it to formulate a practical folding algorithm. To this end, he is developing an algorithm, LINUS, to predict the fold of a protein from its amino acid sequence alone. LINUS is an acronym for Local Independently Nucleated units of Structure. The procedure ascends the folding hierarchy in discrete stages, with concomitant accretion of structure at each step. The chain is represented by simplified geometry and folds under the influence of an extremely simple energy function. Current results are encouraging.