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

Debayan Chakraborty, Yassmine Chebaro & David Wales
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 $\alpha$-helix to a $\beta$-hairpin is critical because it is thought to be a harbinger of amyloid assembly. In this study, we explore the energy landscape for a 18-residue peptide...
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