**Title: Impact of Glycine to Lysine Mutation on Protein Structure****Introduction**A protein has undergone a mutation where glycine is replaced by lysine. This change can significantly affect the protein's structure and function. Understanding these effects is crucial in the study of protein chemistry and molecular biology.**Amino Acids Involved**- **Glycine (Gly, G):** - Structure: Consists of a single hydrogen atom as its side chain, making it the smallest amino acid. - Properties: It's a small, non-polar, hydrophobic molecule that allows flexibility in the protein chain.- **Lysine (Lys, K):** - Structure: Contains a long aliphatic side chain with a terminal amino group, making it larger and polar. - Properties: It is a hydrophilic, basic amino acid that can form ionic bonds due to its positive charge at physiological pH.**Potential Impacts of the Mutation**1. **Hydrophobic to Hydrophilic Change:** - A small hydrophobic amino acid (glycine) is replaced with a large hydrophilic amino acid (lysine), potentially altering the protein folding and stability. This can affect interactions within the protein and with other biomolecules.2. **Folding and Structural Changes:** - The introduction of a bulkier lysine may cause steric hindrance, disrupting the original compact structure if glycine was involved in tight packing. 3. **Chemical Property Differences:** - Differences in size and charge between glycine and lysine mean these residues significantly differ in chemical properties, potentially causing substantial alterations in the protein's function and interactions.4. **Hydrogen Bond Disruption:** - Lysine can form additional hydrogen and ionic bonds due to its side chain, potentially disrupting existing hydrogen bonds and altering the protein's tertiary structure.**Conclusion**Understanding the implications of this mutation helps predict changes in protein function, which is essential for fields such as genetic engineering, drug design, and understanding disease mechanisms.

Answered: Image /qna-images/answer/0c8f20df-e903-4673-aee8-08915c735eed.jpg

A protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H *NH, Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structure

A protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H *NH, Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structure

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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