We are using the Computer Graphics Laboratory resources to design and re-design a four helix bundle protein. The modest resolution crystal structure for this de novo designed four-helix bundle proto-type was recently published. Another crystal form was found which yielded a data set of higher resolution. We are solving this structure now. We will be using this unique structure to understan some of the protein design principles that were originally introduced. Further studies planned include using this new structural data to design mutations using the CGL graphics lab resources such as MidasPlus graphics software and gene manipulation software. The direction of the mutation currently focuses on understanding cooperativity in protein unfolding and what leads to fold specificity. Strictly structural studies will include testing whether this simple protein can be a scaffold for studying protein-protein interactions between loops of difficult to study proteins, such as membrane proteins with well-definited functional loops. Biochemical and structural studies will follow the new proteins designed using the CGL resources. The design will focus on adding function to understand the nature of the basic principles which allow proteins to carry minimal function.
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