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.
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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.
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- The T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.Apohemoglobin (apoHb) is a dimeric globular protein with two vacant heme‐binding. The preparationof apoHb is based on partial hemoglobin (Hb) unfolding to facilitate heme extraction into an organic solvent. What is an appropriate method for removing the heme? a. An acidic buffer to protonate the His axial ligand in the presence of ureaas the denaturing agent. b. An acidic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent. c. A basic buffer to deprotonate the His axial ligand in the presence of ureaas the denaturing agent. d. An basic buffer to protonate the His axial ligand in the presence of mercatoethanol as the denaturing agent.Give 2 structural features in each of the given proteins below that make them perform their biological roles effectively (structural features that directly make them effective in their respective biological roles). Explain how each structural feature directly contributes to proteins’ biological roles. hemoglobin immunoglobulin
- The hemoglobin protein has quaternary structure. This means that hemoglobin Selected answer will be automatically saved. For keyboard navigation, press up/down arrow keys to select an answer. a b C P e is composed of subunits binds to the surface of membranes forms part of the quadruple complex changes over time has four-fold symmetryOne of the alpha helices of hemoglobin beta subunit would represent this type of structure: O PRIMARY O SECONDARY O TERTIARY O QUATERNARYWhich of the following is/are descriptive of all globular proteins? 1. They are significantly hydrophilic in nature. II. They serve as primary scaffolding of cells. III. They are conflation of various types of local folding of polypeptide. Select the correct response: Il only land I Ionly Il and III land IlI I, ll and III Ill only
- Which of the following did Ruth Benesch and her husband Reinhold Benesch accomplish? Select all that apply. determining the function of 2-3-biphosphoglyceric acid determined the exact location BPG binds hemoglobin by X-ray analysis predicted the location BPG binds to hemoglobin demonstrated that the alpha and beta heterodimers of hemoglobin and conformational changes in the protein were essential to the function of the protein and its cooperative bindingThe primary structure of mammalian hemoglobin, an a202 tetramer, is approximately. O 2% 18% Ο 50% Ο 78% 0 986 identical to myoglobinLysozyme consist of 4 disulfide bridges while Bovine Serum Albumin(BSA) is 17. However, lysozyme is more rigid compared to BSA. Why? What are the factors affecting the rigidity of their structures? Does the number of α-helixes and β-sheets matter?
- The steps involved in the T→ R transition in when oxygen binds to hemoglobin are outlined below. Place them in the correct order (1 = first thing to happen), assuming that it is the oxygen-binding that initiates the transition and that the process occurs in discrete steps. The proximal histidine is pulled by the heme iron. The F helix is pulled out of place, breaking a network of salt bridges. The iron is pulled into the plane of the protoporphyrin IX ring. Oxygen binds to the heme. < <Identify the incorrect statement regarding the polypeptide, Myoglobin. Select one: a. The interaction between Myoglobin and O2 is homotopic in nature as indicated by a Hill coefficient n = : 1 b. Myoglobin is found predominantly in muscle tissue because it facilitates oxygen diffusion. c. The majority of Myoglobin's secondary structure is composed of alpha-helices d. Myoglobin has a higher affinity for oxygen than Hemoglobin e. Myoglobin serves as an oxygen storage protein as suggested by its hyperbolic binding of 02The figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent Interactions