Asked Sep 25, 2019

The most important contribution to the stability of a globular protein's conformation appears to be the:

a.) entropy increase from the decrease in ordered water molecules forming a solvent shell around it.

b.) maximum entropy increase from ionic interactions between the ionized amino acids in a protein.

c.) sum of free engeries of formation of may weak interactions between its polar amino acids and surrounding water.


Expert Answer

Step 1

Globular proteins (spheroproteins) are the spherical proteins. Globular proteins are the slightly stable. Since, during the folding of protein into its original conformation, the released free energy is comparatively less. The folding of a specific globular protein is inimitable. It is liable for the exceptional role of that protein.

The hydrophilic amino acid is present on the outer side of the globular proteins. On contact with water, the spherical globes of protein start to dissolve in water. These can form colloids in water. Therefore, the globular proteins are water-soluble to some extent.


Step 2

The correct option is (a).

Dissociation takes place when the atoms or their groups split off from molecules and make ions. It results in the modification of hydrogen bonds. This change in the solvent results in a decrease in overall entropy of the system. In this way, the molecules are more ordered than in liqui...

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