USING NATURALLY OCCURRING PROTEINS AS STABLE SCAFFOLDS FOR STUDYING PROTEIN FOLD

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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.