Molecular origin of constant m-values, denatured state collapse, and residue-dependent transition midpoints in globular proteins.

@article{OBrien2009MolecularOO,
  title={Molecular origin of constant m-values, denatured state collapse, and residue-dependent transition midpoints in globular proteins.},
  author={Edward P O'Brien and Bernard R. Brooks and D. Thirumalai},
  journal={Biochemistry},
  year={2009},
  volume={48 17},
  pages={
          3743-54
        }
}
Experiments show that for many two-state folders the free energy of the native state, DeltaG(ND)([C]), changes linearly as the denaturant concentration, [C], is varied. The slope {m = [dDeltaG(ND)([C])]/(d[C])}, is nearly constant. According to the transfer model, the m-value is associated with the difference in the surface area between the native (N) and denatured (D) state, which should be a function of DeltaR(g)(2), the difference in the square of the radius of gyration between the D and N… CONTINUE READING
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