Work

De NovoDesign of Helical Bundles as Models for Understanding Protein Folding and Function

Year: 2000

Type: review

Abstract: 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.

Source: Accounts of Chemical Research

DOI: 10.1021/ar970004h

Authors: R. Blake Hill, Daniel P. Raleigh, Angela Lombardi, William F. DeGrado

Institutions: Stony Brook University, University of Pennsylvania

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: STRUCTURE AND DYNAMICS OF A NATIVE LIKE DESIGNED PROTEIN