Lecture 2.3: Hemoglobin Variants Flashcards
Fetal hemoglobin: [–] 2,3 BPG = [–] O2 binding = [–] likely to enter [–] -state
decrease 2,3 BPG binding = increase O2 binding = less likely to enter T-state
reduced 2,3 BPG binding = [–] hemoglobin in [–] O2 affinity
more hemoglobin in high O2 affinity state
fetal hemoglobin favors which state?
R state
hemoglobin S (HbS) molecules aggregate forming [–] that cause RBCs to form [–] shape
fibrils, that cause RBCs form sickle shape
sickle cells result in [–] efficency from the [–] to [–]
reduced oxygen transport efficency from lungs to tissue
Glu 6 on beta chains is replaced with a [–] that can interact with [–] areas on other beta subunits
valine, hydrophobic areas
glu is negative and polar!
the hydrophobic areas that interact are only exposed to [–] state
deoxy HbS/ T state
anything that stabilizes the [–] state will [–] the amount of HbS fibers
T state, increases the amount of HbS fibers
Structure of Glycerophospholipids
polar head –> phosphate –> glycerol –> 2 fatty acid tails
sphingolipids structure
choline –> phosphate –> sphingosine + fatty acid tail (ceramide)
or
glycan group (3 sugars) –> sphingosine + fatty acid (ceramide)
cholesterol strcuture
polar head –> steroid ring –> short hydrocarbon tail
Sphingomyelin, a phospholipids in membranes do not contain?
glycerol
What makes a sphingolipid a glycolipid?
one or more sugars linked to the primary hydroxyl of the sphingosine backbone
increased cholestrol = [–] membrane fluidity
decreased
decreased cholesterol = [–] membrane fluditity
increased
