Key result
D2O proves a worse solvent than H2O for protein I27 by altering folding dynamics.
Single-molecule force spectroscopy demonstrates that solvent hydrogen bond strength significantly impacts the folding and chemical reactions of the cardiac titin I27 module.
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Protein processes exhibit distinct responses to solvent H-bond modulation; leaves open physiological translation.
Dougan et al. (2008) studied this question. Substituting H(2)O with D(2)O vs. H(2)O was evaluated on Protein unfolding, collapse, folding, and chemical reaction rates. Substituting H2O with D2O affected protein unfolding, collapse, folding, and chemical reactions, revealing that D2O is a worse solvent than H2O for the protein I27.