1
mmg 404 Questions with Correct Answers |
Updated (100% Correct Answers)
reasons for disease diagnosis Answer: What's wrong with my child?
What's wrong with me? Can it happen the the next child?
reasons for disease prognosis Answer: Severity of the disease
impacts treatments
hemoglobinopthaies Answer: disease of hemoglobin
why are hemoglobinopathies the most common and well known
inherited diseases Answer: heterozygote advantage, blood samples
are easy to obtain, first to be isolated via recombinant DNA
hemoglobin peptide structure Answer: 8 α helical regions, heme
cofactor, HIS 92, Phe42. consists of 2 α and 2 β type globins
where does HIS 92 bind? Answer: at the heme cofactor
how does heme get locked into binding pocket? Answer: Phe42
α type globin Answer: encoded on 16p. codes for ζ, α1, and α2.
β type globin Answer: encoded on 11p. codes for ε, Gγ, Aγ, δ, β
embryonic hemoglobin Answer: zeta 2 epsilon 2
fetal hemoglobin Answer: alpha 2 gamma 2
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adult hemoglobin Answer: alpha 2 beta 2
how many introns and exons does each hemoglobin gene have
Answer: 3 exons and 2 introns
locus control region (LCR) Answer: enhancer. located on 5' of the
first β-type globin genes. similar one located on α gene cluster
what happens when LCR is deleted Answer: no beta globin types
get produced
sickle cell anemia (HbS) Answer: caused by a mutation in β (GAG->
GTG). HbS then creates fibers that distort RBC shape and black
capillaries. gain of function mutation
α thalassemia Answer: due to an uneven sister chromatid at 16p.
causes lost of an α gene
β thalassemia Answer: caused by numerous mutations in β gene,
causing adult hemoglobin to not be expressed
primary protein structure Answer: amino acid sequence
secondary protein structure Answer: helix v β sheet v random coil
tertiary protein structure Answer: folding into 3D structure
quaternary protein structure Answer: protein-protein interaction
primary structure to gene discovery Answer: DFNA and DNFB
© 2025 All rights reserved
mmg 404 Questions with Correct Answers |
Updated (100% Correct Answers)
reasons for disease diagnosis Answer: What's wrong with my child?
What's wrong with me? Can it happen the the next child?
reasons for disease prognosis Answer: Severity of the disease
impacts treatments
hemoglobinopthaies Answer: disease of hemoglobin
why are hemoglobinopathies the most common and well known
inherited diseases Answer: heterozygote advantage, blood samples
are easy to obtain, first to be isolated via recombinant DNA
hemoglobin peptide structure Answer: 8 α helical regions, heme
cofactor, HIS 92, Phe42. consists of 2 α and 2 β type globins
where does HIS 92 bind? Answer: at the heme cofactor
how does heme get locked into binding pocket? Answer: Phe42
α type globin Answer: encoded on 16p. codes for ζ, α1, and α2.
β type globin Answer: encoded on 11p. codes for ε, Gγ, Aγ, δ, β
embryonic hemoglobin Answer: zeta 2 epsilon 2
fetal hemoglobin Answer: alpha 2 gamma 2
© 2025 All rights reserved
, 2
adult hemoglobin Answer: alpha 2 beta 2
how many introns and exons does each hemoglobin gene have
Answer: 3 exons and 2 introns
locus control region (LCR) Answer: enhancer. located on 5' of the
first β-type globin genes. similar one located on α gene cluster
what happens when LCR is deleted Answer: no beta globin types
get produced
sickle cell anemia (HbS) Answer: caused by a mutation in β (GAG->
GTG). HbS then creates fibers that distort RBC shape and black
capillaries. gain of function mutation
α thalassemia Answer: due to an uneven sister chromatid at 16p.
causes lost of an α gene
β thalassemia Answer: caused by numerous mutations in β gene,
causing adult hemoglobin to not be expressed
primary protein structure Answer: amino acid sequence
secondary protein structure Answer: helix v β sheet v random coil
tertiary protein structure Answer: folding into 3D structure
quaternary protein structure Answer: protein-protein interaction
primary structure to gene discovery Answer: DFNA and DNFB
© 2025 All rights reserved
