A linear sequence of amino acids in a peptide or a protein describes its:
| 1. | Primary structure | 2. | Secondary structure |
| 3. | Tertiary structure | 4. | Quaternary structure |
| 1. | It is the sequence of amino acids in a polypeptide chain. |
| 2. | It includes α-helices and β-pleated sheets formed by hydrogen bonds. |
| 3. | It represents the overall three-dimensional structure of a single polypeptide. |
| 4. | It involves interactions between different polypeptide chains or subunits. |
The primary structure of a protein molecule has
| 1. | two ends | 2. | one end |
| 3. | three ends | 4. | no ends |
| List-I | List-II | ||
| A. | Primary structure of protein | I. | Human haemoglobin |
| B. | Secondary structure of protein | II. | Disulphide bonds |
| C. | Tertiary structure of protein | III. | Polypeptide chain |
| D. | Quaternary structure of protein | IV. | Alpha helix and β sheet |
| 1. | A-III,B-IV,C-II,D-I | 2. | A-III,B-II,C-I,D-IV |
| 3. | A-I,B-III,C-II,D-IV | 4. | A-IV,B-III,C-II,D-I |
| 1. | It has a primary, tertiary and quaternary structure only. |
| 2. | It has a primary, secondary and tertiary structure only. |
| 3. | It has a primary and secondary structure only. |
| 4. | It has a primary, secondary, tertiary and quaternary structure. |
| 1. | Primary: amino acid sequence linked by peptide bonds |
| 2. | Secondary: α-helices and β-sheets stabilized by hydrogen bonds |
| 3. | Tertiary: 3D folding through various interactions |
| 4. | All of the above |