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Questions and Answers
What is a characteristic of globular proteins?
What is a characteristic of globular proteins?
- Compact shape with rounded structure (correct)
- Insoluble in water
- Linear shape with irregular structure
- Exclusively perform immune functions
What type of proteins are myoglobin and hemoglobin?
What type of proteins are myoglobin and hemoglobin?
- Glycoproteins
- Conjugated proteins (correct)
- Enzymatic proteins
- Fibrous proteins
What is the function of myoglobin?
What is the function of myoglobin?
- Carrier of oxygen through bloodstream
- Oxygen storage in muscle tissue (correct)
- Motor function in the body
- Regulatory function in the body
Where is hemoglobin found in the body?
Where is hemoglobin found in the body?
What is the prosthetic group in myoglobin and hemoglobin?
What is the prosthetic group in myoglobin and hemoglobin?
What type of structure does myoglobin present?
What type of structure does myoglobin present?
What are the biological functions performed by globular proteins?
What are the biological functions performed by globular proteins?
What gives the name 'heme proteins' to myoglobin and hemoglobin?
What gives the name 'heme proteins' to myoglobin and hemoglobin?
What is the Apoprotein part in myoglobin and hemoglobin?
What is the Apoprotein part in myoglobin and hemoglobin?
What is a prosthetic group in proteins?
What is a prosthetic group in proteins?
What is the main difference between fibrous proteins and globular proteins?
What is the main difference between fibrous proteins and globular proteins?
Which protein is a main component of connective tissue and is the most abundant protein in mammals?
Which protein is a main component of connective tissue and is the most abundant protein in mammals?
What is the general structure of the primary chain of collagen?
What is the general structure of the primary chain of collagen?
What is the consequence of a mutation affecting Collagen type I?
What is the consequence of a mutation affecting Collagen type I?
What causes Scurvy, a condition characterized by symptoms such as small hemorrhages, tooth loss, and poor wound healing?
What causes Scurvy, a condition characterized by symptoms such as small hemorrhages, tooth loss, and poor wound healing?
What is the function of Myosin in muscle cells?
What is the function of Myosin in muscle cells?
What is G-actin considered to be in relation to actin filaments?
What is G-actin considered to be in relation to actin filaments?
What forms the core of the contractile unit on muscle cells?
What forms the core of the contractile unit on muscle cells?
What is the consequence of a lack of Vitamin C in relation to actin filaments and muscle contraction?
What is the consequence of a lack of Vitamin C in relation to actin filaments and muscle contraction?
What is the main function of thin filaments in muscle cells?
What is the main function of thin filaments in muscle cells?
What is the function of hemoglobin in erythrocytes?
What is the function of hemoglobin in erythrocytes?
What is the quaternary structure of hemoglobin?
What is the quaternary structure of hemoglobin?
What is the function of the Heme group in hemoglobin?
What is the function of the Heme group in hemoglobin?
Where is the Heme group positioned in myoglobin?
Where is the Heme group positioned in myoglobin?
What amino acid residues are well-conserved in myoglobin and hemoglobin?
What amino acid residues are well-conserved in myoglobin and hemoglobin?
How many polypeptide chains and heme groups does hemoglobin have?
How many polypeptide chains and heme groups does hemoglobin have?
What type of protein is hemoglobin?
What type of protein is hemoglobin?
How does BPG affect hemoglobin's oxygen binding efficiency?
How does BPG affect hemoglobin's oxygen binding efficiency?
What effect do protons and CO2 have on hemoglobin's affinity for oxygen?
What effect do protons and CO2 have on hemoglobin's affinity for oxygen?
What is the main function of myoglobin?
What is the main function of myoglobin?
Study Notes
Hemoglobin and Myoglobin: Structure and Function
- Hemoglobin in erythrocytes transports oxygen from lungs to tissues and CO2 from tissues to lungs
- Hemoglobin has a quaternary structure with four protein subunits, each containing a prosthetic Heme group
- The Heme group allows for the storage and transportation of oxygen, containing a complex organic ring structure coordinated with an iron atom in its ferrous state
- Myoglobin and hemoglobin both consist of an apoprotein (proteinic part) and a non-proteinic prosthetic group (Heme group)
- Myoglobin's heme group is positioned within a hydrophobic pocket of the apoprotein, protecting it from oxidation and preventing CO from binding
- Specific well-conserved amino acid residues in myoglobin and hemoglobin include Proximal Histidine (His F8) and Distal Histidine (His E7)
- Hemoglobin is an oligomeric protein with 4 polypeptide chains and 4 heme groups, arranged in symmetric pairs without covalent bonds
- Hemoglobin is an allosteric protein, transitioning between T state (no oxygen binding) and R state (oxygen bound) through T to R transition
- Hemoglobin's oxygen binding efficiency is affected by protons, CO2, and 2,3-biphosphoglycerate (BPG)
- Protons and CO2 reduce hemoglobin's affinity for oxygen, promoting oxygen release to tissues and binding of CO2
- BPG affects physiological adaptation to high altitudes by decreasing hemoglobin's oxygen affinity, leading to faster oxygen release
- Fibrous proteins are adapted for structural functions, conferring strength and flexibility to structures where they are present
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Description
Test your knowledge of hemoglobin and myoglobin with this quiz on their structure and function. Explore the intricate details of their roles in transporting oxygen, the impact of specific amino acid residues, the influence of factors like protons, CO2, and BPG on oxygen binding efficiency, and their adaptation to high altitudes.
