title: Switchable proline derivatives: tuning the conformational stability of the collagen triple helix by pH changes.
abstract: (4S)-Aminoproline is introduced as a pH-sensitive probe for tuning the conformational properties of peptides and proteins. The pH-triggered flip of the ring puckering and the formation/release of a transannular H bond were used to switch the formation of collagen triple helices on and off reversibly.
authors.affiliation: Laboratorium für Organische Chemie, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich (Switzerland).
authors.forename: Christiane
authors.initials: C
authors.lastname: Siebler
authors.forename: Roman S
authors.initials: RS
authors.lastname: Erdmann
authors.forename: Helma
authors.initials: H
authors.lastname: Wennemers
mesh_terms: D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D011392:Proline / Q000031:analogs & derivatives*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013237:Stereoisomerism
chemical_list: D003094:Collagen; D011392:Proline
keywords: PPII helix; collagen; proline; ring pucker; stereoelectronic effects