Both myoglobin and hemoglobin are conjugated proteins, they both contain heme wh
ID: 791143 • Letter: B
Question
Both myoglobin and hemoglobin are conjugated proteins, they both contain heme which is a Term 1positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease . In terms of shape, the oxygen binding curve of myoglobin is Term 2positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease and that of hemoglobin is Term 3positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease . When one oxygen molecule is bound to hemoglobin, it becomes easier for the next to bind. This phenomena is called Term 4positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecreaseTerm 5positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease . In these proteins the Term 6positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecreaseTerm 7positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease is seen to coordinate with the heme iron. Bound oxygen coordinates with the heme iron on the other side and the Term 8positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecreaseTerm 9positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease forms a hydrogen bond with the oxygen. Hemoglobin can exist in two conformational states: one is the R state which would be Term 10positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease Hb while the Term 11positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease state would be Term 12positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease Hb. The molecule Term 13positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease binds hemoglobin in its central cavity. The effect of this molecule is to Term 14positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease hemoglobin's affinity for oxygen. Hemoglobin is also influenced by pH. This is called the Term 15positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease effect. A decrease in pH will Term 16positivenegativehistidineproximaldistalcooperativityprosthetic groupoxydeoxyTRBohrBPGhyperbolicsigmoidalchaperoneironmodified amino acidincreasedecrease hemoglobin's affinity for oxygen.
The options are positive, negative, histidine,proximal,prosthetic group,oxy,deoxy,t, R, modified amino acid,chaperone
Explanation / Answer
1) prosthetic group,
2) hyperbolic,
3) sigmoid
4)R(relaxing),
5) cooperativity,
6) proximal
7)distal,
8) histidine,
9)oxy,
10) positive
11) negative,
12)T
13) iron
15) bohr ,
16) increase
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