T-4 Lysozyme as a Model for Protein Folding

本项目的目标是更详细地了解 蛋白质结构、稳定性和 动力学 T4溶菌酶是用作模型的蛋白质。 这 中等大小的蛋白质具有已知的三维结构。 许多 存在这种溶菌酶的突变蛋白，其热力学 稳定性由组合物调节。 达尔奎斯特博士 开发了一种质粒表达系统， 同位素取代的蛋白质，以有效地生产。 他将利用现代核磁共振技术来研究这种 proteins. 蛋白质如何折叠的问题被认为是 最重要也是最不为人所知的 现代分子生物学 一些相关领域将是 通过详细了解为什么 特定的氨基酸序列折叠成特定的形状 以及序列的变化如何改变形状， 热力学稳定性及其与 其他配体。 褶皱作用的研究进展 问题可能允许更可靠的预测结构， 序列数据与相应的增加， 工程蛋白质产品的复杂性。

The goal of this project is to understand in greater detail the interrelationships of protein structure, stability and dynamics. T4 lysozyme is the protein used as a model. This moderate sized protein has a known 3-dimensional structure. Many mutant proteins of this lysozyme exist whose thermodynamic stability is modulated by the composition. Dr. Dahlquist has developed a plasmid expression system which allows large amounts of isotopically substituted protein to be produced efficiently. He will use modern nuclear magnetic resonance to study such proteins. The question of how proteins fold is acknowledged as one of the most important and least understood of modern molecular biology. A number of related areas would be greatly enhanced by the ability to understand in detail why a particular amino acid sequence folds into a particular shape and how changes in sequence change that shape, its thermodynamic stability and its interaction potential with other ligands. Progress in the understanding of the folding problem may allow more reliable predictions of structure from sequence data with a corresponding increase in the sophistication of engineered protein products.