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Globular protein
spherical shaped and somewhat water soluble
Globular protein core
nonpolar, van der waals forces
Globular protein surface
Charged, polar, salt bridges
Globular protein functions
storage of ions and molecules, transport of ions and molecules, defense against pathogens, muscle contraction, biological catalysis
Fibrous proteins
forms long protein filaments, shaped like rods that are typically inert and water-soluble
Actin fold
ATP binds to the middle of the cleft of the actin fold, promoting a change closing the cleft; ATP is cleaved to ADP
Nucleotide binding fold
binding site for NAD+
Hemoglobin
found only in red blood cells, transporting H+ and CO2 from tissues to the lungs and O2 from lungs to tissues
Allosteric effects regulating hemoglobin
pO2, pH/pCO2, 2,3-bisphosphyoglycerate
CO poisoning
CO has a similar size and shape to O2 and can fit to the same binding site, competing with oxygen and blocking the function of myoglobin, hemoglobin, and mitochondrial cytochromes
Fetal hemoglobin (HbF)
major hemoglobin found in newborns with a higher affinity for O2 than HbA; transfers O2 from maternal to fetal circulation across placenta
HbA2
appears shortly before birth
HbA1C
high in patients with diabetes mellitus; undergoes glycosylation, which depends on plasma glucose levels
Sulf-Hb
forms because of high sulfur levels, sulfhemoglobinemia; irreversible
Carboxy-Hb
CO2 replaces O2 and binds 200x faster, carboxyhemoglobin; common in smokers
Met-Hb
contains Fe3+ that cannot deliver O2, methemoglobemia; acquired and congenital, reversible with methylene blue infusion
Hemoglobinopathies
structural defects in hemoglobin, diminished production of one of the two subunits, or abnormal associations of otherwise abnormal subunits
What are major hemoglobinopathies?
Sickle cell disease, thallasemia, hemoglobin C disease, Hemoglobin SC disease