Pages that link to "Q30674756"
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The following pages link to Characterization of the unfolding of ribonuclease a by a pulsed hydrogen exchange study: evidence for competing pathways for unfolding (Q30674756):
Displaying 16 items.
- The Unfolding MD Simulations of Cyclophilin: Analyzed by Surface Contact Networks and Their Associated Metrics (Q27346678) (← links)
- Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration (Q30157052) (← links)
- Multiple folding pathways of the SH3 domain (Q30163959) (← links)
- Direct observation of parallel folding pathways revealed using a symmetric repeat protein system. (Q30364261) (← links)
- Predicting protein backbone chemical shifts from Cα coordinates: extracting high resolution experimental observables from low resolution models. (Q30371096) (← links)
- Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR. (Q36283277) (← links)
- Folding subdomains of thioredoxin characterized by native-state hydrogen exchange (Q36572178) (← links)
- Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state (Q37337994) (← links)
- How cooperative are protein folding and unfolding transitions? (Q38927110) (← links)
- Dry molten globule intermediates and the mechanism of protein unfolding (Q39856385) (← links)
- The effects of cosolutes on protein dynamics: the reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide (Q41910097) (← links)
- Thermal aggregation of ribonuclease A. A contribution to the understanding of the role of 3D domain swapping in protein aggregation (Q44281858) (← links)
- Osmolytes induce structure in an early intermediate on the folding pathway of barstar (Q44982138) (← links)
- Real-time NMR Kinetic Studies Provide Global and Residue-specific Information on the Non-cooperative Unfolding of the β-Trefoil Protein, Interleukin-1β (Q46335426) (← links)
- Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry (Q46933001) (← links)
- A versatile microfluidic chip for millisecond time-scale kinetic studies by electrospray mass spectrometry (Q47304818) (← links)