A multifunnel energy landscape encodes the competing α-helix and β-hairpin conformations for a designed peptide.

Abstract excerpt

Depending on the amino acid sequence, as well as the local environment, some peptides have the capability to fold into multiple secondary structures. Conformational switching between such structures is a key element of protein folding and aggregation. Specifically, understanding the molecular mechanism underlying the transition from an α-helix to a β-hairpin is critical because it is thought to be a harbinger of...

Topics

• Mutation
• Peptides
• Protein Conformation, alpha-Helical
• Protein Conformation, beta-Strand