Inside Cover: (4R)‐ and (4S)‐Fluoroproline in the Conserved cis‐Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering (ChemBioChem 9/2013). Issue 9 (12th June 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: 1018
• Page End: 1018
• Publication Date: 2013-06-12
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201390030
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The inside cover picture shows</bold> the crystal structure of the thioredoxin variant Trx1P, which contains <italic>cis</italic>‐Pro76 as the only proline residue. On <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 1053 ff.</ext-link>, M. Rubini et al. explain how the tertiary structure dictates the <italic>cis</italic> conformation–there is <italic>endo</italic> puckering of the ring when Pro76 is replaced by either (4<italic>R</italic>)‐ or (4<italic>S</italic>)‐fluoroproline, although (4<italic>R</italic>)‐fluoroproline disfavors this conformation.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg21kvgct0" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>