STRUCTURE, FUNCTION & STABILITY OF T4 PHAGE LYSOZYME

结构、功能

• 批准号: 6309031
• 负责人: BRIAN W MATTHEWS
• 金额: $ 2.74万
• 依托单位: UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-02-01 至 2002-01-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6309031
• 关键词: bacteria; bioengineering /biomedical engineering; biomedical resource; biotechnology; virus

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.

SIR提供（L）-TE-MET； 1.8G这是主要目标 建议是使用T4溶菌酶作为模型系统来更好地理解 决定折叠，稳定性，结构和 蛋白质的功能。 要完成的具体研究 包括以下内容：（a）将尝试简化 蛋白质折叠问题通过识别哪些残基或组合 残留物中的T4溶菌酶对于折叠和稳定性至关重要。 我们不仅要了解给定残留物的贡献 稳定性，以及信号（如果有的话）定义的元素 二级结构。 最终我们想减少氨基 T4溶菌酶的酸序列至最简单的形式仍然会给出 折叠的功能性蛋白质。 （b）蛋氨酸取代，一起 与其他非极性替代品一起，将用于更好地理解 对蛋白质折叠至关重要的核心包装相互作用。 （c）将开发和测试方法以提高蛋白质稳定性。 （d）将利用T4溶菌酶内的空腔来理解 蛋白质 - 配体相互作用和工程师新型活性位点。 （E） 蛋白质中应变的作用将进行系统分析。