Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling.

@article{Teilum2002TransientSF,
  title={Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling.},
  author={Kaare Teilum and Birthe B Kragelund and Flemming M. Poulsen},
  journal={Journal of molecular biology},
  year={2002},
  volume={324 2},
  pages={349-57}
}
Paramagnetic relaxation has been used to monitor the formation of structure in the folding peptide chain of guanidinium chloride-denatured acyl-coenzyme A-binding protein. The spin label (1-oxyl-2,2,5,5-tetramethyl-3-pyrroline-3-methyl)methanesulfonate (MTSL) was covalently bound to a single cysteine residue introduced into five different positions in the amino acid sequence. It was shown that the formation of structure in the folding peptide chain at conditions where 95% of the sample is… CONTINUE READING

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