In hemoglobin from patients with sickle cell anemia, the hemoglobin ß-chains have asingle amino substitution that results in:A) A sticky spot in the hemoglobin causing polymerizationO B)A change in the oxygen binding to hemoglobin that causes formation ofpolymersC) Changes in the interaction between B-chains and x-chainsOD) Changes in binding of 2,3-bisphosphoglycerate

Sickle cell anemia is a genetic disease that results in the formation of the sickle shape of RBCs.…

Answered: In hemoglobin from patients with sickle…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section10.7: Defects In Transport Proteins: Hemoglobin

Problem 1EG

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Fetal hemoglobin comprises of αγ sub-units. It has been found that the γ-chain contains serine at position 143 instead of Histidine 143 normally found in the β-chain. The amino acid 143 lines the DPG binding site. This mutation in the γ chain results in a) Increased Oxygen binding in the fetus. b) Increased efficiency of oxygen transport to the lungs in the fetus. c) Increased DPG binding in the fetal hemoglobin d) This is a silent mutation, i.e. no change should be observed.
A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in a) Not enough information b) Normal binding to oxygen c) Higher than normal binding affinity to oxygen d) Lower than normal binding affinity to oxygen
Tay-Sachs disease is result from a)malfunction of cerebroside metabolism b)the accumulation of GM2 c) a defiency of GM2 d) defective lysosomes
The disruption of which of the following interactions directly contributes towards removing 2,3-BPG from HB? a) Tyr 145 - Val 98 b) His 146 - Lys 40 c) His 146 - Asp 94 d) Tyr-145 - His 146
Serum blood of a patient with dislipoproteinemia type 1 has milky appearance even in fasting. If serum stays at low temperature (40) for several hours fatty layer appears on its surface. What are the possible causes of these symptoms? To explain this, answer the questions and do the following tasks: a) what compounds of serum must be tested for that patient in biochemical lab? b) write the reaction which does not occur properly in patient’s blood; c) write down the schemes, explaining how the products of the previous reaction are used in adipose tissue and heart in healthy person 2 hours after a meal.
forskolin is a drug used by scientists to render adenylyl cyclase (AC) constitutively (always) active. What will this do to: a) PKA levels? b) IP3 levels? O a) increase PKA b) no effect on IP3 O a) no effect on PKA b) increase IP3 O a) no effect on PKA b) no effect on IP3 O a) increase PKA b) increase IP3
What signal does the chaperone-mediated autophagy pathway of protein degradation use to identify proteins for destruction? a)The amino acid sequence KFERQ b)HSP90 c)The presence of ubiquitin groups d)The amino acid sequence PEST
Which statement among A-D is false regarding bacterial toxins? A) O Hemolysıns are cell membrane disrupters that can rupture red blood cells. B) O Second mesengar pathway disrupters like cholera toxin produces a debilitating respiratory condition of the lungs. C) O Shiga toxin, tetanus toxin, and hemolysins are all types of exotoxins. D) O Superantigens elicit a hyperactive response by the immune system and can lead to shock. E) O None are false, A-D are all true statements.
Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity (Please provide clear and sufficient explanation for each part, thank you!)
Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity?
In the ubiquitin-proteasome pathway of degradation, what component is most important in determining specificity when selecting proteins for destruction? a)ubiquitin b)E1 ubiquitin-activating enzyme c)E2 ubiquitin-conjugating enzyme d)E3 ubiquitin-protein ligase e)19S proteasome
Which level of protein structure would be most affected by the following changes... a) mutation from isoleucine to valine b) oxidation of two cysteine sidechains c) PrP (healthy prion protein, mostly a-helical) changes to PrP (infectious form, mostly ß-strand) (more than one answer!) d) increase in pH from 7 to 10

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