Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.

@article{Patra2007CharacterizationOT,
  title={Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.},
  author={Ashish K Patra and Jayant B Udgaonkar},
  journal={Biochemistry},
  year={2007},
  volume={46 42},
  pages={11727-43}
}
The mechanisms of folding and unfolding of the small plant protein monellin have been delineated in detail. For this study, a single-chain variant of the natively two-chain monellin, MNEI, was used, in which the C terminus of chain B was connected to the N terminus of chain A by a Gly-Phe linker. Equilibrium guanidine hydrochloride (GdnHCl)-induced unfolding experiments failed to detect any partially folded intermediate that is stable enough to be populated at equilibrium to a significant… CONTINUE READING

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