Side-chain effects on peptidyl-prolyl cis/trans isomerisation.

@article{Reimer1998SidechainEO,
  title={Side-chain effects on peptidyl-prolyl cis/trans isomerisation.},
  author={Ulf Reimer and Gerd Scherer and Mario Drewello and Sebastian Kruber and Mike Schutkowski and Gunter Fischer},
  journal={Journal of molecular biology},
  year={1998},
  volume={279 2},
  pages={449-60}
}
Peptidyl-prolyl cis/trans isomerisation has been frequently found as a rate limiting step in the folding of proteins. In order to determine whether the nature of the amino acid preceding proline controls the probability of cis prolyl bonds in native proteins, systematic studies on the thermodynamics and kinetics of the prolyl isomerisation in the pentapeptide series Ac-Ala-Xaa-Pro-Ala-Lys-NH2 were performed. All proteinogenic amino acids were substituted in the position preceding proline. When… CONTINUE READING

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