biochemistry
if you could please help me answer the following questions!
Homework Answers
21. c. Hemoglobin with oxidized Fe(III) bound to heme which does not bind oxygen
23. d. Daniel Koshland proposed the sequential model of
allostery 
based on 'Induced fit
theory'
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biochemistry
if you could please help me answer the following questions!
EFT i 11) (6 pts)...
biochemistry Question 2.(12 pts) O2 binding to Fe? in one subunit of hemoglobin changes the binding affinity of the...
biochemistry
Question 2.(12 pts) O2 binding to Fe? in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the change in the shape of the heme that results in O2 binding. Page 4/7 b. How is the heme shape change communicated to the other subunits c. What is the role of Bisphosphoglycerate (BPG) in hemoglobin mediated oxygen transport? Question 3.(9 pts) You need to make up a 600 ml of a 40 mM solution...
please answer all. 14. [6 pts) Indicate which of the following statements is True (T) or...
please answer all.
14. [6 pts) Indicate which of the following statements is True (T) or False (F) When water interacts with hydrophobic molecules, it becomes more ordered and entropy of the system increases The hydrophobic effect is predominant in protein stability The Ramachandran ploy shows combinations of dihedral angles in a polypeptide chain. A proteins function is directly related to the protein's secondary structure. The B sheet is primarily stabilized by R group interactions Clusters of secondary structures are...
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy),...
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy), whereas maternal erythrocytes contain HbA (022). Consider the oxygen saturation curve shown below and answer the questions that follow: a) Which hemoglobin has a higher affinity for oxygen? Explain how you made that interpretation. +BPG 0.5 -BPG b) What is the physiological significance of the different 02 affinities? 8 10 4 6 po, kPa) 2. In the context of O, binding...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
biochem help. could i get an explaination on how to get the right answer plz. It...
biochem help. could i get an explaination on how to get the right
answer plz.
It is possible to observe the effect of oxygenation of hemoglobin in an unbuffered solution in distilled water, but it is more common to measure the effect of pH in a bicarbonate-buffered solution (like plasma) on the oxygen affinity of the protein. These are actually the two ways in which the Bohr effect was first described. From what you know about the origin of the...
biochemistry concept I need help with. not a hw question. on our test our professor is...
biochemistry concept I need help with. not a hw question.
on our test our professor is going to ask us something along
the lines of these questions but I just don't understand them even
after reading the questions. I don't understand how to know when to
shift the line to the right vs left.
HEMOGLOBIN Draw the oxygen-binding curve on the graph for A-normal hemoglobin, B normal hemoglobin when BPG levels double and c-a disease that causes high blood oxygenation...
biochemistry if you could please help me answer the following questions! 741) (5 pts) Transition state theory relate...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
Question 31 6 pts 16) Some patients with erythrocytosis (excess Red Blood Cells) have a mutation...
Question 31 6 pts 16) Some patients with erythrocytosis (excess Red Blood Cells) have a mutation that converts a Lysine to Alanine at residue 82 in the beta-subunit of hemoglobin. This particular Lysine normally protrudes in the central cavity of deoxyhemoglobin, where it participates in binding 2,3,-bisphosphoglycerate (BPG). What effect would you predict this mutation will have on a) the affinity of hemoglobin for BPG and for b) the affinity of hemoglobin for Oxygen in patients with erythrocytosis? Briefly explain...
Help 11. About two dozen histidine residues in bemoglobin are involved in binding the protons produced...
Help
11. About two dozen histidine residues in bemoglobin are involved in binding the protons produced by cellular metabolism. In this manner, hemoglobin contributes to buffering in the blood and the imidazole groups able to bind and release protons contribute to the Bohr effect. One important contnbutor to the Bohr effect is His 146 on the β chain of hemoglobin, whose side chain is in close pro to the side chain of Asp 94 in the deoxy form of hemoglobin...
Please help me answer these questions © © 110 | Amo 15% For Question #s 29-34,...
Please help me answer these questions
© © 110 | Amo 15% For Question #s 29-34, refer to the Hb-oxygen dissociation curve at right. 112 Percent hemoglobin saturation mL o, per 100 ml blood 10 20 30 40 50 60 70 80 Po, of blood (mm Hg) 90 100... up to 760 29. The characteristic sigmoid shape of the Hb-oxygen dissociation curve is due to what property of hemoglobin? (2 pts) 30. Identify the Hb Pso for this curve. (2...
biochemistry
Question 2.(12 pts) O2 binding to Fe? in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the change in the shape of the heme that results in O2 binding. Page 4/7 b. How is the heme shape change communicated to the other subunits c. What is the role of Bisphosphoglycerate (BPG) in hemoglobin mediated oxygen transport? Question 3.(9 pts) You need to make up a 600 ml of a 40 mM solution...
please answer all.
14. [6 pts) Indicate which of the following statements is True (T) or False (F) When water interacts with hydrophobic molecules, it becomes more ordered and entropy of the system increases The hydrophobic effect is predominant in protein stability The Ramachandran ploy shows combinations of dihedral angles in a polypeptide chain. A proteins function is directly related to the protein's secondary structure. The B sheet is primarily stabilized by R group interactions Clusters of secondary structures are...
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy), whereas maternal erythrocytes contain HbA (022). Consider the oxygen saturation curve shown below and answer the questions that follow: a) Which hemoglobin has a higher affinity for oxygen? Explain how you made that interpretation. +BPG 0.5 -BPG b) What is the physiological significance of the different 02 affinities? 8 10 4 6 po, kPa) 2. In the context of O, binding...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
biochem help. could i get an explaination on how to get the right
answer plz.
It is possible to observe the effect of oxygenation of hemoglobin in an unbuffered solution in distilled water, but it is more common to measure the effect of pH in a bicarbonate-buffered solution (like plasma) on the oxygen affinity of the protein. These are actually the two ways in which the Bohr effect was first described. From what you know about the origin of the...
biochemistry concept I need help with. not a hw question.
on our test our professor is going to ask us something along
the lines of these questions but I just don't understand them even
after reading the questions. I don't understand how to know when to
shift the line to the right vs left.
HEMOGLOBIN Draw the oxygen-binding curve on the graph for A-normal hemoglobin, B normal hemoglobin when BPG levels double and c-a disease that causes high blood oxygenation...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
Question 31 6 pts 16) Some patients with erythrocytosis (excess Red Blood Cells) have a mutation that converts a Lysine to Alanine at residue 82 in the beta-subunit of hemoglobin. This particular Lysine normally protrudes in the central cavity of deoxyhemoglobin, where it participates in binding 2,3,-bisphosphoglycerate (BPG). What effect would you predict this mutation will have on a) the affinity of hemoglobin for BPG and for b) the affinity of hemoglobin for Oxygen in patients with erythrocytosis? Briefly explain...
Help
11. About two dozen histidine residues in bemoglobin are involved in binding the protons produced by cellular metabolism. In this manner, hemoglobin contributes to buffering in the blood and the imidazole groups able to bind and release protons contribute to the Bohr effect. One important contnbutor to the Bohr effect is His 146 on the β chain of hemoglobin, whose side chain is in close pro to the side chain of Asp 94 in the deoxy form of hemoglobin...
Please help me answer these questions
© © 110 | Amo 15% For Question #s 29-34, refer to the Hb-oxygen dissociation curve at right. 112 Percent hemoglobin saturation mL o, per 100 ml blood 10 20 30 40 50 60 70 80 Po, of blood (mm Hg) 90 100... up to 760 29. The characteristic sigmoid shape of the Hb-oxygen dissociation curve is due to what property of hemoglobin? (2 pts) 30. Identify the Hb Pso for this curve. (2...
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