STRUCTURE, FUNCTION & STABILITY OF T4 PHAGE LYSOZYME

SIR提供了（l）-te-met; 1.8g 建议使用T4溶菌酶作为模型系统，以更好地了解 确定折叠、稳定性、结构和 蛋白质的功能。 要完成的具体研究 （a）将设法简化 蛋白质折叠的问题，通过确定哪些残基，或组合 T4溶菌酶中的氨基酸残基对折叠和稳定性至关重要。 我们不仅想了解给定的残基如何影响 稳定性，但也有信号，如果有的话，定义的元素， 二级结构 最后我们想减少氨基 将T4溶菌酶的酸序列转化为最简单的形式， 一种折叠的功能性蛋白质 (b)甲基取代，一起 与其他非极性替代品，将用于更好地了解 核心-包装相互作用对蛋白质折叠至关重要。 (c)将开发和测试方法以提高蛋白质稳定性。 (d)T4溶菌酶内的空腔将被利用来理解 蛋白质-配体相互作用和设计新的活性位点。 （五） 将系统地分析应变在蛋白质中的作用。

The SIR provided (l)-te-met; 1.8g The principal objective of this proposal is to use T4 lysozyme as a model system to better understand the factors that determine the folding, stability, structure and function of proteins. The specific research to be accomplished includes the following: (a) An attempt will be made to simplify the protein folding problem by identifying which residues, or combinations of residues, in T4 lysozyme are critical for folding and stability. We want to understand not only how given residues contribute to stability, but also the signals, if any, that define the elements of secondary structure. Ultimately we would like to reduce the amino acid sequence of T4 lysozyme to the simplest form that will still give a folded, functional protein. (b) Methionine substitution, together with other nonpolar replacements, will be used to better understand the core-packing interactions that are critical to protein folding. (c) Methods will be developed and tested to improve protein stability. (d) Cavities within T4 lysozyme will be exploited both to understand protein-ligand interaction and to engineer novel active sites. (e) The role of strain within the protein will be systematically analyzed.