1988/08/19 by Lynne Regan, William F. DeGrado · 8 citations
Biochemistry, Genetics and Molecular Biology · #Protein Structure and Dynamics #Chemical Synthesis and Analysis #RNA and protein synthesis mechanisms
paper · doi:10.1126/science.3043666
openalex publication_date 1988/08/19 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.