title: (4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold: tertiary structure context dictates ring puckering.
abstract: Fine-tuning protein stability: The non-natural amino acids (2S,4R)- and (2S,4S)-fluoroproline modulate protein stability by biasing the proline ring pucker and the cis/trans equilibrium of prolyl peptide bonds. We incorporated both fluoroproline stereoisomers at the invariant cis-proline residue of the thioredoxin fold. The results show that tertiary structure context overrules the conformational preferences of fluoroprolines.
authors.affiliation: Department of Organic Chemistry/Cellular Chemistry, University of Konstanz, Universitätsstrasse 10, 78464 Konstanz, Germany. marina.rubini@uni-konstanz.de
authors.forename: Marina
authors.initials: M
authors.lastname: Rubini
authors.forename: Martin A
authors.initials: MA
authors.lastname: Schärer
authors.forename: Guido
authors.initials: G
authors.lastname: Capitani
authors.forename: Rudi
authors.initials: R
authors.lastname: Glockshuber
mesh_terms: D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D010084:Oxidation-Reduction; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry; D015202:Protein Engineering; D058849:Protein Refolding; D058767:Protein Unfolding; D013237:Stereoisomerism; D013816:Thermodynamics; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
chemical_list: C431803:fluoro-proline; D013879:Thioredoxins; D011392:Proline