Protein Structure and Folding at Low Temperature

了解蛋白质如何以及为什么折叠成它的 天然构象具有重要的生物学意义。 尽管在这个问题上已经做了很多工作， 对这一过程的细节知之甚少。 芬克博士正在研究决定一个特定的 折叠途径和天然结构。 长期 目标是了解氨基酸的“规则”， 多肽的序列引导折叠路径到多肽的末端。 本土国家。 Fink博士将使用：用途：1）特定信号或 分子不同区域的探针 确定蛋白质折叠和展开的顺序; 2)位点特异性突变体，以促进 蛋白质与环境敏感探针在独特的， 选择位点并探测单个氨基酸的作用 酸的折叠;和3）零度以下的温度， 含水甲醇低温溶剂以允许稳定化， 在两种方法中部分折叠的中间体的表征 展开和重折叠。

An understanding of how and why a protein folds into its native conformation is of major biological importance. Although much work has been done on this problem still relatively little is known about the details of the process. Dr. Fink is studying the factors which determine a particular folding pathway and hence native structure. The long-term goals are to learn the "rules" by which the amino acid sequence of a polypeptide guides the folding path to the native state. Dr. Fink will use: 1) specific signals or probes in different regions of the molecule to aid determining the order in which the protein folds and unfolds; 2) site-specific mutants to facilitate the formation of protein with environment-sensitive probes in unique and selected sites and probe the role of individual amino acids on the folding; and 3) subzero temperatures and aqueous-methanol cryosolvents to permit the stabilization and characterization of partially-folded intermediates in both unfolding and refolding.