Making extensive use of polymer chemistry concepts, it has recently been claimed that water is a good solvent for the denatured state of globular proteins [J. Mol. Biol. 432 (2020) 2882]. Here, I discuss how overinterpretation of classical polymer chemistry should be avoided and how recent ideas about the source of the hydrophobic effect can explain the role of water in the folding and conformational stability of globular proteins.
Is water a good solvent for the denatured state of globular proteins?
Graziano G.
2020-01-01
Abstract
Making extensive use of polymer chemistry concepts, it has recently been claimed that water is a good solvent for the denatured state of globular proteins [J. Mol. Biol. 432 (2020) 2882]. Here, I discuss how overinterpretation of classical polymer chemistry should be avoided and how recent ideas about the source of the hydrophobic effect can explain the role of water in the folding and conformational stability of globular proteins.File in questo prodotto:
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