During folding, bonds between the protein’s amino acids and water molecules (intermolecular bonds) are replaced by bonds between the amino acids (intramolecular bonds). Thus, folding causes only small changes of both enthalpy and entropy and hence free energy (marginal stability of proteins). This allows reversible changes of protein structure upon ligand binding or changes in the environmental conditions.

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Folding and Unfolding of Proteins

  • Engelbert Buxbaum

摘要

During folding, bonds between the protein’s amino acids and water molecules (intermolecular bonds) are replaced by bonds between the amino acids (intramolecular bonds). Thus, folding causes only small changes of both enthalpy and entropy and hence free energy (marginal stability of proteins). This allows reversible changes of protein structure upon ligand binding or changes in the environmental conditions.