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HbA glutamic acid interacts with negatively charged regions interacts with positively charged regions ᎻᏏ valine hydrophobic Answer Bank forms covalent bonds interacts with chemically similar regions negatively charged Hb lysine positively charged

HbA glutamic acid interacts with negatively charged regions interacts with positively charged regions ᎻᏏ valine hydrophobic Answer Bank forms covalent bonds interacts with chemically similar regions negatively charged Hb lysine positively charged

Human Anatomy & Physiology (11th Edition)
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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The most common allele of the β chain of hemoglobin in humans, ???,H⁢bA, has glutamic acid at the sixth position. Two different amino acid substitutions at the sixth position produce two variants, ???H⁢bS and ???,H⁢bC, of the sickle‑cell allele. The ???H⁢bS allele occurs when valine is substituted for glutamic acid, and the ???H⁢bC allele occurs when lysine is substituted for glutamic acid. To answer the question, refer to the amino acid table.

Match the class of amino acid and the chemical property to each possible amino acid. Not all answers will be placed.

**Transcription for Educational Website:** **Title:** Amino Acid Interactions and Characteristics **Overview:** This educational image provides an interactive exercise to explore the properties and interactions of specific amino acids linked to hemoglobin: glutamic acid, valine, and lysine. Each amino acid is associated with a type of hemoglobin: \( Hb^A \) for glutamic acid, \( Hb^S \) for valine, and \( Hb^C \) for lysine. **Interactive Boxes:** - **\( Hb^A \) Glutamic Acid** - **\( Hb^S \) Valine** - **\( Hb^C \) Lysine** **Answer Bank:** Below the boxes, there is an "Answer Bank" containing descriptions of interactions and characteristics. The goal is to match these with the appropriate amino acid: - Interacts with negatively charged regions - Forms covalent bonds - Interacts with chemically similar regions - Positively charged - Interacts with positively charged regions - Hydrophobic - Negatively charged **Instructions:** Users should drag descriptions from the Answer Bank into the corresponding boxes to correctly identify the properties and possible interactions of each amino acid in the context of its role in hemoglobin. This exercise links biochemical properties with genetic variations in hemoglobin. **Note:** Emphasis is placed on understanding how the chemical nature of these amino acids influences their function and interaction within biological systems, such as blood oxygen transport, sickle cell anemia, and other hemoglobinopathies.
Transcribed Image Text:**Transcription for Educational Website:** **Title:** Amino Acid Interactions and Characteristics **Overview:** This educational image provides an interactive exercise to explore the properties and interactions of specific amino acids linked to hemoglobin: glutamic acid, valine, and lysine. Each amino acid is associated with a type of hemoglobin: \( Hb^A \) for glutamic acid, \( Hb^S \) for valine, and \( Hb^C \) for lysine. **Interactive Boxes:** - **\( Hb^A \) Glutamic Acid** - **\( Hb^S \) Valine** - **\( Hb^C \) Lysine** **Answer Bank:** Below the boxes, there is an "Answer Bank" containing descriptions of interactions and characteristics. The goal is to match these with the appropriate amino acid: - Interacts with negatively charged regions - Forms covalent bonds - Interacts with chemically similar regions - Positively charged - Interacts with positively charged regions - Hydrophobic - Negatively charged **Instructions:** Users should drag descriptions from the Answer Bank into the corresponding boxes to correctly identify the properties and possible interactions of each amino acid in the context of its role in hemoglobin. This exercise links biochemical properties with genetic variations in hemoglobin. **Note:** Emphasis is placed on understanding how the chemical nature of these amino acids influences their function and interaction within biological systems, such as blood oxygen transport, sickle cell anemia, and other hemoglobinopathies.
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