Ionization State of Glutamate and Protein Folding

Very Hard Organic Chemistry Biological Molecules

Consider the structure of biomolecules, specifically focusing on different types of amino acids and their roles in protein structure and function. The amino acid glutamate can be protonated or deprotonated depending on the pH of the surrounding environment. At physiological pH (approximately 7.4), glutamate predominantly exists in its deprotonated form, which influences its interaction with other molecules.

Which of the following statements is the MOST accurate regarding the effects of pH on the ionization state of glutamate and its implications for protein folding?

At low pH, glutamate is predominantly protonated, gaining a positive charge that stabilizes protein tertiary structure.

At neutral pH, glutamate exists primarily in its zwitterionic form, enabling it to form strong hydrogen bonds with nearby polar residues.

The deprotonated form of glutamate at physiological pH can engage in electrostatic interactions with positively charged amino acids.

Altering the pH to above 9 causes glutamate to become negatively charged, disrupting its role in maintaining protein structure.

Hint

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