1995/11/10 by James W. Bryson, Stephen F. Betz, Helen S. M. Lu +4 · 3 citations
Biochemistry, Genetics and Molecular Biology · #Protein Structure and Dynamics #Chemical Synthesis and Analysis #RNA and protein synthesis mechanisms
paper · doi:10.1126/science.270.5238.935
openalex publication_date 1995/11/10 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
The de novo design of peptides and proteins has recently emerged as an approach for investigating protein structure and function. Designed, helical peptides provide model systems for dissecting and quantifying the multiple interactions that stabilize secondary structure formation. De novo design is also useful for exploring the features that specify the stoichiometry and stability of alpha-helical coiled coils and for defining the requirements for folding into structures that resemble native, functional proteins. The design process often occurs in a series of discrete steps. Such steps reflect the hierarchy of forces required for stabilizing tertiary structures, beginning with hydrophobic forces and adding more specific interactions as required to achieve a unique, functional protein.