Ontology highlight
ABSTRACT:
SUBMITTER: Baker EG
PROVIDER: S-EPMC5860740 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Nature chemical biology 20170522 7
Miniproteins simplify the protein-folding problem, allowing the dissection of forces that stabilize protein structures. Here we describe PPα-Tyr, a designed peptide comprising an α-helix buttressed by a polyproline II helix. PPα-Tyr is water soluble and monomeric, and it unfolds cooperatively with a midpoint unfolding temperature (T<sub>M</sub>) of 39 °C. NMR structures of PPα-Tyr reveal proline residues docked between tyrosine side chains, as designed. The stability of PPα is sensitive to modif ...[more]