Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH

@article{Chamberlain1996DetectionOR,
  title={Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH},
  author={Aaron Keith Chamberlain and Tracy M. Handel and Susan Marqusee},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={782-787}
}
Despite the general observation that single domain proteins denature in a completely cooperative manner, amide hydrogen exchange of ribonuclease H in low levels of denaturant demonstrates the existence of two partially folded species. The structures of these marginally stable species resemble kinetic folding intermediates and the molten globule state of the protein. These data suggest that the first region to fold is the thermodynamically most stable portion of the protein and that the molten… 
The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
TLDR
Results indicate that the first portion of ribonuclease HI to fold is the most thermodynamically stable region of the native state, and that folding of this protein follows a hierarchical process.
Confirmation of the hierarchical folding of RNase H: a protein engineering study
TLDR
Results indicate that interactions formed in the intermediate persist in the transition and native states and that RNase H folds through a hierarchical mechanism.
Folding of an isolated ribonuclease H core fragment
TLDR
It is shown indirectly that the monomeric form of eABCD is folded and has an overall secondary structure similar to the dimeric form.
Native-state energetics of a thermostabilized variant of ribonuclease HI.
TLDR
Though increased in stability by a uniform factor, D10A shows a distribution of stabilities in its secondary structural units that is similar to that of E. coli RNase H, but not the closely related protein from Thermus thermophilus, Hence, the simple mutation used to stabilize the enzyme does not recreate the balance of conformational flexibility evolved in the thermophilic protein.
The energetics of T4 lysozyme reveal a hierarchy of conformations
TLDR
The overall subdomain hierarchy of energies does not mirror data on the folding pathway for this protein, challenging the relationship between energy landscapes and folding trajectories.
Hydrogen exchange studies of protein structure.
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