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?

Salt bridges (ionic interactions)

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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. Lysine and aspartate can form salt bridges. Occur between negatively charged and positively charged amino acid side chain groups. Occur between hydrocarbon side chains of amino acids. Alanine and isoleucine can form salt bridges. They can also stabilize quaternary structure by bringing together two polypeptide chains. 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.

Explanation / Answer

Answer - Oppositely charged side chains can attract each other, forming salt bridges.

1. Lysine and aspartate can form salt bridges. Lysine +ve charge and Asp negative charge makes ionic interaction or salt bridge.

2. Occur between negatively charged and positively charged amino acid side chain groups.

3. They can also stabilize quaternary structure by bringing together two polypeptide chains.

4. 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.

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