Myoglobin binding of oxygen depends on: Select one: O a. the oxygen concentration O b. the...
Tertiary structure is maintained by Select one: o peptide bond o hydrogen bond o disulphide bond o all of the above Myoglobin binding of oxygen depends on: Select one: O a. the oxygen concentration O b. the haemoglobin concentration O c. the affinity of myoglobin for the oxygen d. a) and c) e. a), b) and c) Amino acid residues commonly found in B-turns are: Select one: o alanine (Ala) and glycine (Gly). O two cysteine (Cys) residues. o proline...
Which of the following statements is/are TRUE? Select one: O A. Heme is part of the secondary structure of myoglobin. O B. The distal histidine assists in heme binding to myoglobin. O C. Oxygen binds to the proximal histidine. O D. All of the above statements are true O E. None of the above statements are true
Hemoglobin: binds oxygen with a higher affinity than myoglobin due to the presence of four heme groups vs. only one in myoglobin. binds oxygen with a lower affinity than myoglobin due to the presence of four heme groups vs. only one in myoglobin. binds to oxygen with a lower affinity than myoglobin due to the presences of the T-state that is absent in myoglobin. binds to oxygen with a higher affinity than myoglobin due to the presences of the R-state...
high afinia sizmold binding curve llustrate the presence of a low affinity stat and a high -affinity state? 8. Compare and contrast the "T" and "R" state 9. True or false? o The histidine in myoglobin covalently binds oxygen. o The iron in heme of myoglobin binds the oxygen atom of CO. o The tertiary structure of myoglobin is similar to that of a subunit of hemoglobin. o The quaternary structure of myoglobin is similar to that of a subunit...
001 Select all answers that can correctly complete the following statement The sigmoidal shape of hemoglobin's oxygen binding curve indicates that Select one or more: a. hemoglobin binds oxygen with different affinities. b. hemoglobin is saturated with oxygen over a narrow range oxygen concentrations. c. oxygen binding is cooperative. d. hemoglobin is mixed with myoglobin. e. oxygen binds with the same affinity at all concentrations. Nex
Binding of oxygen to both myoglobin and hemoglobin in causes a conformational change in which a proximal histidine is moved toward the plane of the heme ring. In hemoglobin, this results in a sigmoidal O2 binding whereas myoglobin exhibits hyperbolic O2 binding. Explain this difference.
41. Which of the following statements about protein-ligand binding is correct? A) The K is equal to the concentration of ligand when all of the binding sites are occupied. B) The K is independent of such conditions as salt concentration and pH. C) The larger the K. (association constant), the weaker the affinity. D) The larger the K. the faster is the binding. E) The larger the K, the smaller the K. (dissociation constant) 42. The ability of O, to...
1) Select all that apply. Globular proteins: a)are found in hair and wool. b)include myoglobin and collagen. c)are usually water soluble. d)aggregate in aqueous media. e)are often made of β-pleated sheet and α-helix sections wrapped into compact structures. 2) Select all that apply. The Bohr effect: a)depends on the atomic orbital structure of hydrogen. b)can be summarized as a reduction in the oxygen affinity of hemoglobin with decreasing pH. c)is explained by the protonation of key amino acids, including the...
Which of the following binding will decrease binding of O, to hemoglobin? Select one: a. all of the listed b. CO2 c. BPG d. CO e. H+ де
1. How can hemoglobin deliver oxygen to myoglobin in muscle tissue cells? (use oxygen binding curve, T-state and R-state, sigmoidal, cooperativity, Bohr effect, carbon dioxide, and 2,3-BPG)