Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 33, Issue 11, Pages 745-754Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar970004h
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Funding
- NIGMS NIH HHS [F32 GM018491, F32 GM018491-01] Funding Source: Medline
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De novo protein design has proven to be a powerful tool for understanding protein folding, structure, and function. In this Account, we highlight aspects of our research on the design of dimeric, four-helix bundles. Dimeric, four-helix bundles are found throughout nature, and the history of their design in our laboratory illustrates our hierarchic approach to protein design. This approach has been successfully applied to create a completely native-like protein. Structural and mutational analysis allowed us to explore the determinants of native protein structure. These determinants were then applied to the design of a dinuclear metal-binding protein that can now serve as a model for this important class of proteins.
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