Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.

@article{Hodsdon2001IntestinalFA,
  title={Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.},
  author={Michael E. Hodsdon and Carl Frieden},
  journal={Biochemistry},
  year={2001},
  volume={40 3},
  pages={732-42}
}
The intestinal fatty acid binding protein is composed of two beta-sheets surrounding a large interior cavity. There is a small helical domain associated with the portal for entry of the ligand into the cavity. Denaturation of the protein has been monitored in a residue-specific manner by collecting a series of two-dimensional (1)H-(15)N heteronuclear single-quantum coherence (HSQC) NMR spectra from 0 to 6.5 M urea under equilibrium conditions. In addition, rates for hydrogen-deuterium exchange… CONTINUE READING

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