How do the following noncovalent interactions help to stabilize the tertiary and

Question

How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein?

Hydrophobic interactions

Check all that apply.

Occur between negatively charged and positively charged amino acid side chain groups. Occur between hydrocarbon side chains of amino acids. Lysine and aspartate take part in hydrophobic interactions. They can stabilize the tertiary structure of a protein by connecting two distant parts of a polypeptide chain or by pulling the protein backbone together in the middle of the chain. In a protein, these side chains cluster in the center of the molecule to exclude water, and are responsible for the nearly spherical tertiary shape of globular proteins. They can also stabilize quaternary structure by bringing together two polypeptide chains. Alanine and isoleucine take part in hydrophobic interactions.

Explanation / Answer

1. The statement 1 is false.

Reason: There exist hydrophilic interactions between the negatively charged and the positively charged amino acid side chain groups.

2. The statement 2 is true.

3. The statement 3 is false.

Reason: Lysine is a positively charged amino acid, whereas aspartate is a negatively charged amino acid.

4. The statement 4 is true.

5. The statement 5 is true.

6. The statement 6 is false.

Reason: The quaternary structure refers to how these protein subunits interact with each other and arrange themselves to form a larger aggregate protein complex. The final shape of the protein complex is once again stabilized by various interactions, including hydrogen-bonding, disulfide-bridges and salt bridges.

7. The statement 7 is true.

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