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Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline

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2015

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Roderer, Daniel
Glockshuber, Rudi

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https://doi.org/10.1002/cbic.201500342
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ChemBioChem. 2015, 16(15), pp. 2162-2166. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201500342

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The incorporation of the non-natural amino acids (4R)- and (4S)-fluoroproline (Flp) has been successfully used to improve protein stability, but little is known about their effect on protein folding kinetics. Here we analyzed the influence of (4R)- and (4S)-Flp on the rate-limiting trans-to-cis isomerization of the Ile75-Pro76 peptide bond in the folding of Escherichia coli thioredoxin (Trx). While (4R)-Flp at position 76 had essentially no effect on the isomerization rate in the context of the intact tertiary structure, (4S)-Flp accelerated the folding reaction ninefold. Similarly, tenfold faster trans-to-cis isomerization of Ile75-(4S)-Flp76 relative to Ile75-Pro76 was observed in the unfolded state of Trx. Our results show that the replacement of cis prolines by non-natural proline analogues can be used for modulating the folding rates of proteins with cis prolyl-peptide bonds in the native state.

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540 Chemie

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ISO 690RODERER, Daniel, Rudi GLOCKSHUBER, Marina RUBINI, 2015. Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline. In: ChemBioChem. 2015, 16(15), pp. 2162-2166. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201500342
BibTex
@article{Roderer2015Accel-32629,
  year={2015},
  doi={10.1002/cbic.201500342},
  title={Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline},
  number={15},
  volume={16},
  issn={1439-4227},
  journal={ChemBioChem},
  pages={2162--2166},
  author={Roderer, Daniel and Glockshuber, Rudi and Rubini, Marina}
}
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    <dcterms:abstract xml:lang="eng">The incorporation of the non-natural amino acids (4R)- and (4S)-fluoroproline (Flp) has been successfully used to improve protein stability, but little is known about their effect on protein folding kinetics. Here we analyzed the influence of (4R)- and (4S)-Flp on the rate-limiting trans-to-cis isomerization of the Ile75-Pro76 peptide bond in the folding of Escherichia coli thioredoxin (Trx). While (4R)-Flp at position 76 had essentially no effect on the isomerization rate in the context of the intact tertiary structure, (4S)-Flp accelerated the folding reaction ninefold. Similarly, tenfold faster trans-to-cis isomerization of Ile75-(4S)-Flp76 relative to Ile75-Pro76 was observed in the unfolded state of Trx. Our results show that the replacement of cis prolines by non-natural proline analogues can be used for modulating the folding rates of proteins with cis prolyl-peptide bonds in the native state.</dcterms:abstract>
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