(4R)‐ and (4S)‐Fluoroproline in the Conserved cis‐Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering. Issue 9 (27th May 2013)

• Record Type: Journal Article
• Authors: Rubini, Marina; Schärer, Martin A.; Capitani, Guido; Glockshuber, Rudi
• Is Part Of: Chembiochem. Volume 14:Issue 9(2013)
• Page Start: 1053
• Page End: 1057
• Publication Date: 2013-05-27
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201300178
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Fine‐tuning protein stability:</bold> The non‐natural amino acids (2<italic>S</italic>, 4<italic>R</italic>)‐ and (2<italic>S</italic>, 4<italic>S</italic>)‐fluoroproline modulate protein stability by biasing the proline ring pucker and the <italic>cis</italic>/<italic>trans</italic> equilibrium of prolyl peptide bonds. We incorporated both fluoroproline stereoisomers at the invariant <italic>cis</italic>‐proline residue of the thioredoxin fold. The results show that tertiary structure context overrules the conformational preferences of fluoroprolines.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg21kvggtj" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>