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Inside Cover: (4 R )‐ and (4 S )‐Fluoroproline in the Conserved cis ‐Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering (ChemBioChem 9/2013)
Author(s) -
Rubini Marina,
Schärer Martin A.,
Capitani Guido,
Glockshuber Rudi
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201390030
Subject(s) - chemistry , stereochemistry , proline , context (archaeology) , ring (chemistry) , peptide , thioredoxin , peptide bond , biology , biochemistry , enzyme , amino acid , paleontology , organic chemistry
The inside cover picture shows the crystal structure of the thioredoxin variant Trx1P, which contains cis ‐Pro76 as the only proline residue. On p. 1053 ff. , M. Rubini et al. explain how the tertiary structure dictates the cis conformation–there is endo puckering of the ring when Pro76 is replaced by either (4 R )‐ or (4 S )‐fluoroproline, although (4 R )‐fluoroproline disfavors this conformation.