Draw a picture that represents your understanding of why hemoglobin is considered an allosteric protein.
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- describe hemoglobin is a protein composed of four polypeptide chainsNa+K+ATPase and hemoglobin are examples of _____________ proteins.Which 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.
- What amino acid residue interacts with molecular oxygen (O2) in hemoglobin? a. Phenylalanine b. Serine c. Valine d. HistidineThe amino acid in Hemoglobin that is most found to be most sensitive to pH changes, and hence affects Oxygen binding process around pH 7 is Valine Tyrosine Histidine Aspartic AcidWhy picric and tannic acid is used for the treatments of burn. Explain this in the concept of proteins.
- Which of these statements about hemoglobin is NOT true? A) it is a tetrameric globular protein b) it has a prosthetic group called heme c) it’s dominant motif is beta barrel d) its dominant motif is helix-turn-helix The reagent used to break disulfide bonds is: a) urea b) beta-mercaptoethanol c) guanidine hydrochloride d) phosphorus pentachlorideWhat impact do mutations in the alpha-chain usually have, if any, on hemoglobin's function? A. T-to-R-state transition B. dimer-dimer stabilization C. Allosteric Regulation D. A & B E. A & C F. A,B, & CAt low salt concentration, proteins are less soluble
- The isomerization of glucose-6-phosphate yields the molecule __________________________.The affinity of hemoglobin for oxygen varies according to the pH of the plasma. In fact, the warmer and more acidic your blood is, the more likely it is that hemoglobin will let go of oxygen. Explain, in terms of the secondary and tertiary structure of protein why this would be so.Which of these amino acids could be found in the transmembrane portion of a protein? a) asparticacid b) cysteine c) glycine d)isoleucine e) proline