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(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering

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2013

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Schärer, Martin
Capitani, Guido
Glockshuber, Rudi

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ChemBioChem. 2013, 14(9), pp. 1053-1057. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300178

Zusammenfassung

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.

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540 Chemie

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cis peptide bonds, fluoroprolines, proline ring puckers, protein engineering, protein structures

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ISO 690RUBINI, Marina, Martin SCHÄRER, Guido CAPITANI, Rudi GLOCKSHUBER, 2013. (4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering. In: ChemBioChem. 2013, 14(9), pp. 1053-1057. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201300178
BibTex
@article{Rubini2013-06-174Sflu-24514,
  year={2013},
  doi={10.1002/cbic.201300178},
  title={(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering},
  number={9},
  volume={14},
  issn={1439-4227},
  journal={ChemBioChem},
  pages={1053--1057},
  author={Rubini, Marina and Schärer, Martin and Capitani, Guido and Glockshuber, Rudi}
}
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