Protein folding is a thermodynamically favorable process under physiological conditions because:
1- There is a decrease in entropy of the solvent by burying hydrophobic groups within the molecule.
2- No intermediate stage disulphide bonds form during the folding process.
3- There is an increase in entropy associated with protein folding.
4- Of the large negative enthalpy change associated with many noncovalent interactions.
5- All of the above.
Protein folding is a thermodynamically favorable process under physiological conditions because:
1- There is a decrease in entropy of the solvent by burying hydrophobic groups within the molecule.
2- No intermediate stage disulphide bonds form during the folding process.
3- There is an increase in entropy associated with protein folding.
4- Of the large negative enthalpy change associated with many noncovalent interactions.
5- All of the above.
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