Immune-mediated myositis (IMM) is a muscle wasting disease that occurs in quarter horses with an E317G mutation in myosin II. Which is a true statement about the E317G mutation's effect on myosin Il in IMM?

Human Anatomy & Physiology (11th Edition)
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ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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Immune-mediated myositis (IMM) is a muscle wasting
disease that occurs in quarter horses with an E317G
mutation in myosin II. Which is a true statement about
the E317G mutation's effect on myosin Il in IMM?
Select one:
a. The mutation changes the amino acid side chain from a long negatively
charged side chain to a short hydrophobic side chain, which destabilizes
the folding of myosin II, making it more susceptible to degradation and
triggering an autoimmune response to the muscle.
b. The mutation changes the amino acid side chain from a short
hydrophobic side chain to a long negatively charged side chain, which
destabilizes the folding of myosin II, making it more susceptible to
degradation and triggering an autoimmune response to the muscle.
O c. The mutation changes the amino acid side chain from a long negatively
charged side chain to a short hydrophobic side chain, which stabilizes the
folding of myosin II, making it less susceptible to degradation and
protecting the muscle from an autoimmune response.
d. The mutation changes the amino acid side chain from a long negatively
charged side chain to a short uncharged polar side chain, which
destabilizes the folding of myosin II, making it more susceptible to
degradation and triggering an autoimmune response to the muscle.
Transcribed Image Text:Immune-mediated myositis (IMM) is a muscle wasting disease that occurs in quarter horses with an E317G mutation in myosin II. Which is a true statement about the E317G mutation's effect on myosin Il in IMM? Select one: a. The mutation changes the amino acid side chain from a long negatively charged side chain to a short hydrophobic side chain, which destabilizes the folding of myosin II, making it more susceptible to degradation and triggering an autoimmune response to the muscle. b. The mutation changes the amino acid side chain from a short hydrophobic side chain to a long negatively charged side chain, which destabilizes the folding of myosin II, making it more susceptible to degradation and triggering an autoimmune response to the muscle. O c. The mutation changes the amino acid side chain from a long negatively charged side chain to a short hydrophobic side chain, which stabilizes the folding of myosin II, making it less susceptible to degradation and protecting the muscle from an autoimmune response. d. The mutation changes the amino acid side chain from a long negatively charged side chain to a short uncharged polar side chain, which destabilizes the folding of myosin II, making it more susceptible to degradation and triggering an autoimmune response to the muscle.
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