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) | Zendy

Rubini Marina | Zendy; Schärer Martin A. | Zendy; Capitani Guido | Zendy; Glockshuber Rudi | Zendy

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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.

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