The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions

@article{Raschke1997TheKF,
  title={The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions},
  author={Tanya M. Raschke and Susan Marqusee},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={298-304}
}
Folding of ribonuclease HI from Escherichia coli populates a kinetic intermediate detectable by stopped-flow circular dichroism. Pulse labelling hydrogen exchange reveals that this intermediate consists of a structured core region of the protein, namely helices A and D and β-strand 4. This kinetic intermediate resembles both the acid molten globule of ribonuclease HI and rarely populated, partially unfolded forms detected under native conditions. These results indicate that the first portion of… 
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In the molten globule of flavodoxin, the helical region comprising residues Leu110-Val125 is shown to be better protected against exchange than the other ordered parts of the folding intermediate, causing its context-dependent stabilization against unfolding.
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TLDR
Experimental comparisons with non-folding polypeptide chains show that, for ribonuclease A and cytochrome c, these signals reflect a shift from one biased ensemble of the unfolded state to another as a function of change in denaturant concentration.
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.
Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H.
TLDR
This work has characterized the folding process of Thermus thermophilus ribonuclease H using circular dichroism, fluorescence, and pulse-labeling hydrogen exchange, and found that unlike other thermophilic proteins, which unfold much more slowly than their mesophilic counterparts, T.thermophilus RNase H folds and unfolds with overall rates similar to those of E.coliRNase H.
Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism.
3.4 Intermediates in Protein Folding
The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H.
The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure.
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