Imagine there is a beaker with a solution containing 1,000 hemoglobin homotetramers and 1,000 protons (H⁺). Which of the statements concerning the concerted and sequential models is NOT true if you assume only 1 proton is capable of binding 1 hemoglobin monomer?Select one:- a. If an additional 1,000 protons were added, according to the concerted model, all of the homotetramers will adopt the R state.- b. According to the concerted model, the addition of protons will cause an increase in the number of tetramers in the T state.- c. According to the sequential model, there will be some monomers of homotetramers in the R state and some in the T state.- d. If an additional 2,000 protons were added, according to the sequential model, there will be a greater proportion of hemoglobin in the T state.- e. If an additional 2,000 protons were added, according to the concerted model, more hemoglobin will adopt the T state.

Hemoglobin is a protein found in the red blood cells that are involved in the transport of carbon…

Answered: Imagine there is a beaker with a…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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You have discovered a new hemoglobin variant you are calling Hb-21. You have noticed the following from your studies of Hb-21: - The binding constant of Hb-21 is the same at pH 7.1 and 7.4.- The binding constant curves generated by Hb-21 and O2 are sigmoidal.- The Hill coefficient for Hb-21 is 3.-The binding constant for Hb-21 with O2 in the presence of 5mM 2,3-bisphosphglycerate is about 6-times lower instead of the 8-times lower that is observed under these conditions for the wild type enzyme. Use this information to answer questions: Based on this information which of these features of hemoglobin would you conclude are altered in Hb-21 as compared to the wild type hemoglobin? ____ the cooperativity.____ the amount of T versus R state in the tissues. ____ the Bohr effect. What is the major issue for an individual with the Hb-21 variant? Explain exactly what aspect of hemoglobin’s function is altered.
1. Each "20-mg" capsule of Prozac contains 22.5 mg of fluoxetine HCL (m.w. 345.63) equivalent to 20 mg of fluoxetine base. Calculate the molecular weight of the fluoxetine base. Round your answer to the HUNDRETHS decimal place. 2. Each "100-mg" tablet of Imitrex contains 140 mg of sumatriptan succinate equivalent to 100 mg sumatriptan base. If the molecular weight of sumatriptan succinate is 413.5, calculate the molecular weight of sumatriptan base. Round your answer to the HUNDRETHS decimal place.
Draw the GC base pair at pH 10.
The fosfomycin disc (200/50) also contains glucose-6-phosphate (G-6-P). Which ONE of the following best describes why this is the case? Select one: A. G-6-P increases the solubility of fosfomycin B. G-6-P is used to promote active transport of fosfomycin into the bacterial cell C. G-6-P is used in the formulation to correct glucose deficiencies promoted by fosfomycin D. G-6-P stabilises fosfomycin from spontaneous hydrolysis in aqueous solution E. G-6-P is an inhibitor of FosA that inactivates fosfomycin
Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)Which of the following statements about hemoglobin is most consistent with the information in the passage? Group of answer choices A. a tertiary protein with two polypeptides B. a quaternary protein with two polypeptides C. a tertiary protein with four polypeptides D. a quaternary protein with four polypeptides When nucleotides polymerize to form a nucleic acid, ________. Group of answer choices A. a…
In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?
On the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…
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 02
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).
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.
Which of the following statements are TRUE? Multiple answers:Multiple answers are accepted for this question PLEASE SHOW WORK FOR EACH PART AND EXPLAIN WHY EACH ANSWER CHOICE IS WRONG OR RIGHT a. The tripeptide His-Lys-Glu has a net charge of -2 at pH 8.0. b. The tripeptide Asp-Asp-Asp has a net charge of -3 at pH 7.0. c. The tetrapeptide His-His-His-His has a net charge of -1 at pH 7.0. d. There are 6 possible sequences for a tripeptide containing Arg - His - and Pro. e. Certain bacteria synthesize cyclic tetrapeptides. The net charge at pH 7.0 of a cyclic tetrapeptide consisting of two Pro and two Tyr is 0.

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