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• W2071307561 abstract "A lot of research has been performed in the area of protein folding and denaturation. Although different denaturing salts are commonly used to induce the unfolding process, salt-specific effects on protein structure remain controversial despite decades of research. in this work, we combine accurate multi-parameter single-molecule Förster Resonance Energy Transfer (smFRET) experiments, Circular Dichroism (CD) measurements and explicit-water Molecular Dynamics (MD) simulations to investigate salt-specific effects on a short charged α-helix peptide." @default.
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• W2071307561 date "2012-01-01" @default.
• W2071307561 modified "2023-09-26" @default.
• W2071307561 title "How Proteins Unfold" @default.
• W2071307561 doi "https://doi.org/10.1016/j.bpj.2011.11.270" @default.
• W2071307561 hasPublicationYear "2012" @default.
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