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Molecular dynamic (MD) simulations of the model protein Trp‐cage dissolved in 35% ethanol‐water at 298 K have been carried out using conventional force fields. The goal was to develop a better understanding of experimental intermolecular nuclear Overhauser effects (NOEs) that arise from interactions of ethanol methyl groups with hydrogens of the peptide. Cross‐relaxation terms (
) for peptide...
Conformations of the designed peptide Betanova in 42% trifluoroethanol/water (v/v) were explored. Circular dichroism (CD) observations provided no evidence for the presence of significant amounts of β‐structures in water, in TFE/water, or in ethanol/water. Nuclear magnetic resonance (NMR) diffusion experiments showed no significant difference in the hydrodynamic radius of the peptide in water and...
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