Which of the following contributes the most to the stability of the conformation of a water-soluble, globular protein? sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein. entropy increase from the decrease in the number of ordered water molecules forming a solvent shell around the unfolded protein. sum of free energies of formation of many weak interactions between a protein's polar amino acids and surrounding water. maximum enthalpy increase from ionic interactions between the ionized amino acids in a protein. stabilizing effect of hydrogen bonding in a protein between the carbonyl group of one peptide bond and the amino group of another

Chemistry: The Molecular Science
5th Edition
ISBN:9781285199047
Author:John W. Moore, Conrad L. Stanitski
Publisher:John W. Moore, Conrad L. Stanitski
Chapter10: Fuels, Organic Chemicals, And Polymers
Section: Chapter Questions
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Which of the following contributes the most to the stability of the conformation of a
water-soluble, globular protein?
sum of free energies of formation of many weak interactions among the
hundreds of amino acids in a protein.
entropy increase from the decrease in the number of ordered water molecules
forming a solvent shell around the unfolded protein.
sum of free energies of formation of many weak interactions between a protein's
polar amino acids and surrounding water.
maximum enthalpy increase from ionic interactions between the ionized amino
acids in a protein.
stabilizing effect of hydrogen bonding in a protein between the carbonyl group
of one peptide bond and the amino group of another
Transcribed Image Text:Which of the following contributes the most to the stability of the conformation of a water-soluble, globular protein? sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein. entropy increase from the decrease in the number of ordered water molecules forming a solvent shell around the unfolded protein. sum of free energies of formation of many weak interactions between a protein's polar amino acids and surrounding water. maximum enthalpy increase from ionic interactions between the ionized amino acids in a protein. stabilizing effect of hydrogen bonding in a protein between the carbonyl group of one peptide bond and the amino group of another
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