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Questions and Answers
What is the primary cause of Sickle Cell Anemia?
What do secondary structures of proteins refer to?
Which level of protein structure is affected by the abnormality causing genetic diseases?
Which protein is the most abundant in the human body?
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What causes the polypeptide backbone to form regular arrangements of amino acids?
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What vitamin is required as a reducing agent for the hydroxylation of proline and lysine in collagen biosynthesis?
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Which connective tissue disorder is characterized by impaired structural integrity in the skeleton, eye, and cardiovascular system?
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Where is elastin primarily found in the human body?
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What is the main function of myoglobin (Mb) in the body?
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What is the primary function of hemoglobin (Hb) in the body?
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Which hereditary hemolytic disease is characterized by decreased synthesis of β-chains?
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What are the sources that supply amino acids to the amino acid pool?
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What process requires molecular oxygen, Fe2+, and vitamin C (ascorbic acid)?
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What is the primary characteristic of thalassemia?
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What is one of the main functions of elastin in the human body?
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Sickle Cell Anemia is caused by the replacement of polar glutamate with nonpolar valine in the b-subunit of hemoglobin.
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The primary structure of a protein refers to the linear sequence of amino acids.
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Secondary structures of proteins refer to random three-dimensional structures of the polypeptide backbone.
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What does scurvy result in due to a lack of proline and lysine hydroxylation?
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Abnormalities in the primary structure of proteins do not cause any genetic diseases.
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Collagen is a globular protein found in the extracellular matrix, the vitreous humor of the eye, and bone.
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The biosynthesis of collagen involves the hydroxylation of proline and lysine, which requires molecular oxygen, Fe2+, and the reducing agent vitamin C (ascorbic acid).
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Ascorbic acid deficiency can lead to a decrease in the tensile strength of collagen fibers due to impaired interchain hydrogen-bond formation.
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Elastin is primarily found in the walls of large arteries and the elastic ligaments.
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Myoglobin (Mb) is a heme protein present in heart and skeletal muscle and consists of multiple polypeptide chains.
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Hemoglobin (Hb) consists of two identical dimers: (αβ)1 and (αβ)2, and it is primarily found in white blood cells.
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Thalassemia is characterized by decreased synthesis of both α-chains and β-chains.
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The amino acid pool is supplied by the degradation of body proteins, dietary protein, and the synthesis of nonessential amino acids.
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The amino acid pool is depleted by the conversion of amino acids to glucose, glycogen, fatty acids, ketone bodies, or CO2 + H2O.
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The digestion of dietary proteins involves bicarbonate (HCO3-) and pancreatic enzymes.
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Elastin can be stretched to several times its normal length but does not recoil to its original shape when the stretching force is relaxed.
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Nitrogen balance is determined by the input to and output from the amino acid pool.
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