MCB Lec 12

red blood cell protien that is a teramer and a allosteric protien

a single polypetide chain, w a lot of a-helixes, single bound heme and not cooperitive bonding, it binds to oxygen in muscle cells

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cooperitivy enhances oxygen delivery by hemoglobin so that even though it doesnt pick up more O2 it delivers more O2 than myoglobin

the position of the iron atom so the resisdues of aa can hit confirmation angles

release of reactive oxygen species and the interaction between iron and oxygen exists as resonance

they bind oxygen in heme groups and protoporphirin, the centrel iron can bind with imdazome the histidine side group and the sixth cordination is w oxygen

changes the electronic structure of iron making its magnetic properties change
deoxyhemoglobin> oxohemoglobin

the magnetic properties of the heme iron changes when it moves into the polyphorpin ring and MRi can distinguishtthe amount od oxy and deoxyhemoglibin

by pulling the four subunits of the T state closer changing them into the R state when they get closer(15 degrees)

is composed of 2alpha and 2 beta subuinits makng it have a higher affinity for oxygen

produces oxygen via the Bohr effect

Hemoglobin, this is why carbon monoxide poising is dangerous because the hemeglobin more readily uptakes CO2 than O2, treated via hyperbaric oxygen therapy

causer by a mutation in hemoglobin making it harder to produce more iron, the patch will polymerize and create a hydrophobic region

fewer red blood cells and less functional hemoglibin

the a-chain is not producesd in sufficent quantity making the hemoglobin have a lower affinity with O2

the b-chain is not produced in sufficent quantity making hemoglobin insouluble

alpha-hemoglobin stabalizing protien

more preffered

a log-log plot for binding data for o2 binding log(y(1/Y) is ploted against the logO2