Theoretical Studies of Protein Folding

Scheraga博士正在进行一项联合实验， 理论研究计划，旨在阐明能源 和多肽链折叠成 蛋白质的天然构象，以及 在底物上产生的蛋白质（酶或激素），或 受体的 虽然目前的潜在功能是足够的 准确的几个应用程序，他已经提出，他的 这些潜力的分析（以及 文学）表明，现在是时候为一个全新的面貌 在底层形式（和参数化的 这是我们工作的第一个目标。 其次，已经开发出一些非常成功的方法， 克服了小多肽的多重最小值问题， 他将致力于改善这些措施， 它们变成球状蛋白质， 残基 他将在螃蟹和牛身上试验这种方法 胰蛋白酶抑制剂，然后用它们来计算 干扰素的结构 他还将处理大型集会 纤维蛋白质，即胶原蛋白。

Dr. Scheraga is carrying out a combined experimental and theoretical research program designed to elucidate the energies and mechanism of the folding of a polypeptide chain into the native conformation of a protein, and of the action of the resulting protein (enzyme or hormone) on a substrate or receptor. While current potential functions are sufficiently accurate for several of the applications that he has made, his analysis of these potentials (and also of others in the literature) indicates that it is time for a completely new look at the underlying form ( and parameterization of the potentials); this is the first goal of the proposed work. Secondly, some very successful methods have been developed to surmount the multiple-minima problem for small polypeptides and he will devote his efforts to improving them, and extending them to globular proteins containing of the order of 100 residues. He will test the methods on crambin and bovine pancreatic trypsin inhibitor, and then use them to compute the structure of interferon. He will also treat large assemblies of fibrous proteins, viz. collagen.