10. Lack of flexibility can be deadly. pOz in tissues po, in lungs 1.0 Curve 1 A) The hemoglobin protein is “flexible" and can transition between wo states. What are these two “states" Match each state to the appropriate curve in the graph shown. Curve 2 0.8 0.6E 0.4- 3) Explain how binding of oxygen helps hemoglobin transition between these two states. (Think about the “breathing" motions of nemoglobin.) Curve 3 0.2 12 16 C) What are the structural differences between these two states? pO2 (kPa) Figure1a Lennger icipesofeche y. Seven Edon

10. Lack of flexibility can be deadly. pOz in tissues po, in lungs 1.0 Curve 1 A) The hemoglobin protein is “flexible" and can transition between wo states. What are these two “states" Match each state to the appropriate curve in the graph shown. Curve 2 0.8 0.6E 0.4- 3) Explain how binding of oxygen helps hemoglobin transition between these two states. (Think about the “breathing" motions of nemoglobin.) Curve 3 0.2 12 16 C) What are the structural differences between these two states? pO2 (kPa) Figure1a Lennger icipesofeche y. Seven Edon

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've discovered a new organism that contains a mutant form of Hemoglobin (red line on right) and are testing its properties in a lab setting at a neutral pH. You've generated the binding data below comparing it to the wildtype (non-mutant; blue line on left) form. Oxygen binding of a new hemoglobin mutant 1.00 - 0.75- Hemoglobin 0.50 - Wildtype Mutant 0.25- 0.00 - 25 50 75 100 pO2 (torr) 1. How does this mutation seem to impact cooperativity? Hint. Look at the slope of the line. [ Select ] 2. Which variant, the mutant or wildtype, has a higher affinity for oxygen? [ Select ] 3. Which variant is a more effective delivery system to the the muscles (~20 torr)? Select ] Fraction of Hb bounw with Oxygen
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hillcoefficient? Explain your answers.
Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2
5. A 70 kg adult could meet her/his entire energy needs for a day by eating 3 moles of glucose (540 g; molecular weight of glucose is 180 g/mol). Each molecule of glucose generates approximately 36 molecules of ATP when oxidized to CO,. The concentration of ATP in cells is about 5mM, and a 70 kg adult has about 25 liters of intracellular fluid. A. Given that the ATP concentration remains constant in cells, calculate how many times per day, on average, each ATP molecule in the body is hydrolyzed and resynthesized. Show calculations.
Ethanol or Lactic acid G3P Руruvat Glucose G3P Руruvat Acetyl-CoA Citric Acid Охaloacetate
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
1. Hemoglobin researchers have discovered more than 500 naturally occurring hemoglobin mutations. The majority of these results from single amino acid changes. Some of these mutations result in clinical illness or symptoms, but many show no outward effects. Some examples are: HbS (sickle cell Hb)-substitutes Val for Glu on the surface Hb Cowtown - eliminates an ion pair used in T-state stabilization Hb Memphis - surface uncharged polar aa for another of similar size on the surface Hb Bibba-substitutes a Pro for a Leu in an α-helix Hb Milwaukee - substitutes a Glu for a Val Hb Providence- substitutes a Asn for a Lys that normally projects into the central cavity Hb Philly - substitutes a Phe for a Tyr, disrupting hydrogen bonding at the aß interface. EXPLAIN your choices for each of the following: a) The Hb variant least likely to cause pathological symptoms b) The variant(s) most likely to show pl values different from that of HbA c) The variant(s) most likely to show…