USING NATURALLY OCCURRING PROTEINS AS STABLE SCAFFOLDS FOR STUDYING PROTEIN FOLD

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 该提案包含三个项目，涉及基因工程蛋白质，旨在解决蛋白质折叠和稳定性问题。第一个项目解决了淀粉样蛋白形成序列的侧链如何通过将这些序列掺入T4溶菌酶来溶解这些序列而相互作用的问题。第二个项目解决了次级结构构件的上下文依赖性问题。最后一个项目通过研究主链和侧链原子的移动的幅度和方向来解决蛋白质内部的可塑性，这些移动是由于自动化设计在T4溶菌酶的情况下提出的突变而发生的。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This proposal contains three projects involving genetically engineered proteins designed to address questions about protein folding and stability. The first project addresses the question of how the sidechains of amyloid forming sequences interact by solublizing these sequences via their incorporation in T4 lysozyme. The second project addresses questions about of the context dependence of secondary structural elements. The last project addresses the plasticity of protein interiors by studying the magnitude and direction of shifts in backbone and side chain atoms that occur in response to mutations suggested by automated design in the case of the T4 lysozyme.