QUESTION 10 Which of the following proteins does not have quaternary structure? O A. human adult hemoglobin B. myoglobin O C. IgG D. hemoglobin S E. fetal hemoglobin
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- What can be deduced from the following information? N- C- Protein Nonpolar polar acidic basic term term 33 42 10 15 Ser Asp Y 33 42 10 15 Ser Asp A. The two proteins, X and Y are one and the same B. The two proteins are globular proteins that are hydrophilic C. The two proteins are most likely localized in the cytoplasm D. X and Y most likely have transport function for various types of metabolites E. The data is inconclusive and similarity or differences between X and Y cannot be determinedWhich of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environmentsWhich of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.
- Which of the following best explains why fetal hemoglobin (HbF) has higher affinity for oxygen than HbA? a. HbF binds 2,3-bisphosphoglycerate with lower affinity b. One of the coordination positions of HbF is occupied by an Asp residue c. Oxygen binding is not cooperative in HbF d. The Fe-O bond is shorter in HbF e. The hemes of HbF and HbA have different structureserly in alcohol H&E stained sections demonstrate poor contrast between nucleus and cytoplasm. All are preventative or corrective actions EXCEPT a. monitoring water pH due to agricultural run-off b. dehydrating and clearing tissues completely before infiltrating with paraffin c. properly differentiating in alkaline and alcohol solutions d. Allowing eosin to stand in higher concentrations of alcoholsIf there was a molecule that causes Hb to be more stable in the T state, this molecule would: a. Generally, raise the affinity of Hb for O2 b. Generally, lower the affinity of Hb for O2 c. Generally, cause Mb to favor the R state while Hb is in the T state d. Generally, cause Hb to dissociate into αβ dimers
- The classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109erythrocytes will form a monolayer of area 0.89 m2when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2in area. Show that these data can be accounted for only if the erythrocyte membrane is a bilayer.The first step of the lysozyme reaction (catalytic mechanism) is shown in the figure below. Which statement regarding lysozyme is true? Glu 35 HO O(NAM) R (NAG) Asp 52 a. The local environment of Asp 52 significantly changes its pka. b. Glu 35 has an unusually low pKa due to its hydrophobic environment. c. Glu 35 provides acid/base assistance during catalysis. d. Glu 35 acts as a nucleophile during catalysis.The classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109 erythrocytes will form a monolayerof area 0.89 m2 when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2 in area.Show that these data can be accounted for only if the erythrocyte membraneis a bilayer.
- Both simple dufusion and facilitated diffusion of small polar uncharged molecule Select one: O A. all of the choices O B. require the hydrolysis of ATP O C. occur down a concentration gradient (downhill) O D. require carrier proteins O E. occur in animal cells but not in plant cellsList 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms2. j The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding of oxygen to hemoglobin would be altered by the change in conditions noted. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 po2 pO2