Pages that link to "Q41911404"
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The following pages link to How long does it take to equilibrate the unfolded state of a protein? (Q41911404):
Displaying 12 items.
- Theoretical and computational validation of the Kuhn barrier friction mechanism in unfolded proteins (Q33670312) (← links)
- Protein folding as a complex reaction: a two-component potential for the driving force of folding and its variation with folding scenario (Q35596188) (← links)
- Extracting intrinsic dynamic parameters of biomolecular folding from single-molecule force spectroscopy experiments (Q35667903) (← links)
- First passage analysis of the folding of a β-sheet miniprotein: is it more realistic than the standard equilibrium approach? (Q37727675) (← links)
- Recollection (Q39721368) (← links)
- Simulating Replica Exchange: Markov State Models, Proposal Schemes, and the Infinite Swapping Limit (Q40958993) (← links)
- Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics (Q41812654) (← links)
- Probing the origins of two-state folding (Q42111938) (← links)
- Solvent-Exposed Salt Bridges Influence the Kinetics of α-Helix Folding and Unfolding (Q42151733) (← links)
- RNA folding kinetics using Monte Carlo and Gillespie algorithms. (Q47737296) (← links)
- Origins of the Mechanochemical Coupling of Peptide Bond Formation to Protein Synthesis. (Q52631960) (← links)
- First Passage Times, Lifetimes, and Relaxation Times of Unfolded Proteins. (Q53392383) (← links)