Complete the sentence to make it true. The single most important contribution to the stability of a water soluble globular protein's conformation appears to be the 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
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Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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Chapter1: Chemical Foundations
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Complete the sentence to make it true. The single most important contribution to
the stability of a water soluble globular protein's conformation appears to be the
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:Complete the sentence to make it true. The single most important contribution to the stability of a water soluble globular protein's conformation appears to be the 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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