How strong are side chain interactions in the folding intermediate?

@article{Samatova2009HowSA,
  title={How strong are side chain interactions in the folding intermediate?},
  author={Ekaterina N. Samatova and Natalia S Katina and Vitaly A Balobanov and Bogdan S. Melnik and Dmitry A. Dolgikh and Valentina E. Bychkova and Alexei V. Finkelstein},
  journal={Protein science : a publication of the Protein Society},
  year={2009},
  volume={18 10},
  pages={2152-9}
}
Influence of 12 nonpolar amino acids residues from the hydrophobic core of apomyoglobin on stability of its native state and folding intermediate was studied. Six of the selected residues are from the A, G and H helices; these are conserved in structure of the globin family, although nonfunctional, that is, not involved in heme binding. The rest are nonconserved hydrophobic residues that belong to the B, C, D, and E helices. Each residue was substituted by alanine, and equilibrium pH-induced… CONTINUE READING