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Given the equivalence between the EV limit and highly denatured states, our ability to simulate conformational ensembles in the EV limit, with full atomic detail, has direct bearing on the development of an accurate physical picture of conformations accessible to denatured proteins
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All fluorescence spectra were corrected for background scattering as measured with pure buffer
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The preceding study (12) has demonstrated that the creation of hydrophobic ANS binding sites in ice, accounting for the spectral blue shift and intensity enhancement, is owed to partial disruption of the protein tertiary structure triggered by the solidification of water
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This trend is consistent with a pronounced binding capacity of oligomers whose subunits tend to dissociate in frozen aqueous media thereby making accessible large hydrophobic patches of the subunit interface
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Global structure and dynamics of recombinant human Apolipoprotein CII in complex with SDS micelles: evident for increased helix mobility in the binding/activation site for lipoprotein lipase
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New fluorescent probes for the measurement of cell membrane viscosity
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Although the exact time of disk reconstitution varies for apA-2 from different pools, our data consistently show that the vesicle-to-disk conversion after heat denaturation of apoA-2:DMPC disks is a slow reaction that takes hours to complete at 24°C
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This method was successfully tested for biomolecular simulations of peptide folding (Schäfer et al
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Time-resolved FRET (trFRET) measurements were subsequently used to resolve and quantify the equilibrium distribution of extended and docked ribozyme conformers (N
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Ribozyme constructs were prepared in 50 mM Tris/HCl (pH 7
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