The interior of water-soluble globular proteins is shielded from the aqueous environment. This non-polar, hydrophobic environment favors the burial of hydrophobic amino acid residues to minimize unfavorable interactions with water.
We need to identify the most hydrophobic amino acid among the options:
Valine, being a strongly hydrophobic residue, is the most likely to be found in the protein's interior, away from the surrounding water.
| Column I | Column II |
|---|---|
| P. Amylose | 1. $\beta$ ($1\to 4$) |
| Q. Sucrose | 2. $\alpha$ ($1\to 4$) |
| R. Amylopectin | 3. $\alpha 1\to \beta 2$ |
| S. Cellulose | 4. $\alpha$ ($1\to 4$), $\alpha$ ($1\to 6$) |
| Column I | Column II |
|---|---|
| P. Lectins | 1. Acts as ATP dependent pump to efflux out small molecules |
| Q. P-glycoprotein | 2. Targets lysosomal enzymes to their destination |
| R. Digitoxigenin | 3. Specific carbohydrate binding proteins |
| S. Mannose 6-phosphate | 4. Inhibits Na$^+$-K$^+$ pump |
| Monosaccharide | Epimer |
| P. D-mannose | 1. C-3 epimer of D-glucose |
| Q. D-allose | 2. C-4 epimer of D-glucose |
| R. D-galactose | 3. C-4 epimer of D-mannose |
| S. D-talose | 4. C-2 epimer of D-glucose |
| 5. C-5 epimer of D-glucose |