Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation.

@article{Neet1994ConformationalSO,
  title={Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation.},
  author={Kenneth E. Neet and David E Timm},
  journal={Protein science : a publication of the Protein Society},
  year={1994},
  volume={3 12},
  pages={
          2167-74
        }
}
The conformational stability of dimeric globular proteins can be measured by equilibrium denaturation studies in solvents such as guanidine hydrochloride or urea. Many dimeric proteins denature with a 2-state equilibrium transition, whereas others have stable intermediates in the process. For those proteins showing a single transition of native dimer to denatured monomer, the conformational stabilities, delta Gu (H2O), range from 10 to 27 kcal/mol, which is significantly greater than the… CONTINUE READING
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