10. In an abnormal hemoglobin variant known as Hemoglobin-Kariya, the lysine residues at position 40 in the ß-chains are replaced by glutamic acid residues. a) What effect would you expect this change to have on the quaternary structure and oxygen binding properties of hemoglobin?
Q: calculate the length in (in nm) of a 100-residue segment of the α-keratin coiled coil
A: The α-helix in proteins has 3.6 amino acids per turn and a pitch (the distance needed for one…
Q: f) Identify -R groups that: Are hydrophobic, hydrophilic and aromatic • Are the H-bond donors and…
A: In the study of peptides and proteins, understanding their structural and chemical properties is…
Q: a. What is the classification of the Arabinose in terms of combined no. of carbons and highest…
A: The five-carbon sugar arabinose is extensively distributed in nature and can be the only carbon…
Q: A receptor-ligand complex has a dissociation constant of Kd = 20 nM. The rate of receptor-ligand…
A: The reverse rate constant (k-1) is a parameter used in chemical kinetics to describe the rate at…
Q: If, in addition to the constraints on glucose concentration listed previously, we have in the liver…
A: To determine the theoretical concentration of glucose-6-phosphate at equilibrium in a liver cell…
Q: Put these three molecules in the order of most oxidized to least oxidized. нн нс-с-н нн H > > 0=…
A: In chemistry, the concept of oxidation state plays a crucial role in assessing the degree of…
Q: Complete the data missing from the table, which shows assay data from the purification protocol of a…
A: A protein purification assay will include multiple protein purification techniques, conducted one…
Q: Draw the amino acids serine and threomine bonded together with a petide bond.
A: Amino acid
Q: EXPLAIN WHY THE DIRECTION OF MOVEMENT OF FLUID IN THE MANOMETER WAS DIFFERENT DURING YEAST…
A: A manometer measures pressure differences in fluid-filled systems. You seem to be asking about…
Q: Briefly explain partition coefficients. How is this concept applied in biotechnology?
A: The partition coefficient is defined as the concentration of the solute in the hydrophobic phase…
Q: A lysine is on the surface of a protein near an arginine, how does this alter pKa of lysine
A: The pKa of an amino acid's side chain determines whether it is protonated (+) or deprotonated (-)…
Q: Refer to the figure below, what are the following forces of attraction is involved in the protein…
A: The tertiary structure of the protein is a 3D structure established and stabilised by the…
Q: can you tell what the pKas are from this unknown amino acid based on buffering regions and narrow…
A: pH = If [H+] concentration in a solution is high, the pH will be low and the solution is acidic. If…
Q: Below is a U-tube experiment with a membrane that is selectively permeable to water, but does not…
A: Here we are using a U-tube. The height of water column in both tubes are the same, so the force…
Q: 12. Enzymes are biocatalysts that speed up a chemical reaction in biological systems. The path from…
A: Proteins are large high molecular weight molecules and have diverse functional roles to play in a…
Q: Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has p?ap�a values of…
A: Isoleucine is non-polar aliphatic amino acid. Amino acids are biomolecules that have an amino group…
Q: What is the IUPAC name for the following molecule? Sc
A: IUPAC nomenclature rules for alkanes:• Identify the longest continuous carbon chain.• Identify the…
Q: Indicate which of the amino acid residues in the following peptide sequence contains a group that…
A: Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…
Q: For a particular reaction, AH = -16.1 kJ/mol and AS° = −21.8 J/(mol·K). Assuming these values change…
A: To determine the temperature at which the reaction changes from nonspontaneous to spontaneous in the…
Q: What would spread (fragmented) bands in the electrophoresis gel tell you about the quality of your…
A: Gel electrophoresis is a technique used to separate DNA fragments according to their size. The DNA…
Q: Protein A will fold into its native state only when protein B is also present in the solution.…
A: b. Protein B serves as a molecular chaperone for protein A.In this scenario, where protein A can…
Q: 1. In a catabolic pathway, metabolite X gets converted into metabolite Y, metabolite X metabolite…
A: is the standard change in Gibbs free energy i.e. the change in Gibbs free energy under standard…
Q: Where is the active site for this enzyme located?
A: Active site of an enzyme is the part of the enzyme where substrate molecules bind and undergo a…
Q: Would the base pair Guanosine and Cytosine be more or less stable at pH 10
A: The stability of a base pair like Guanosine (G) and Cytosine (C) can be influenced by pH, but in the…
Q: For the equilibrium below, pKa₁ = 7.9 and pKa2 = 10.1. At what pH is [HA] equal to [A²-]?
A: pH of any acid or base tells us its hydrogen ion concentration.PKa- it is that pH when the 50%…
Q: Select All True Statements as It Relates to the Structure Below. CH₂OH HOH2C EXE HO OH OH Г The…
A: The Compound Formed is the Result of a Reaction Between Glycerol and Amino Acid. Glycerol (a polyol…
Q: +40mV -70mV 2 3₂ OmV 4 ich concet Resting Potential 2 froar points to the dupy Time…
A: Electrical signals are how neurons communicate. Electrical signals are generated when there is a…
Q: net charge of this peptide at a pH of 1, 7, and 15
A: PKa value is actually a number which denotes the pH at which a group is half deprotonated. It…
Q: How can molecular structural analysis be accomplished with electrospray ionization mass…
A: Molecular structural analysis involves determining the arrangement and properties of atoms within a…
Q: The equilibrium constant of a system, K, can be related to the standard free energy change, AG,…
A: Details
Q: Step 6 of the citric acid cycle is shown. Which statement best describes the role of FAD in this…
A: Citric acid cycle is a metabolic pathway that regenerates oxaloacetate from citrate. Acetyl CoA from…
Q: The hexokinase can be inhibited by a non competitive inhibitor. On your enzyme show where the non…
A: Hexokinase catalyzes the reaction of glucose binding to ATP to form glucose 6 phosphate. The…
Q: Illustrate the ATP hydrolysis reaction, its regeneration and the AG for both reactions. Show where…
A: ATP is the energy currency of the cell. It is simply an adenosine molecule bonded to a triphosphate.…
Q: Draw a diagram of the hydrogen bonding interactions in: i) a two-stranded antiparallel beta sheet,…
A: Secondary structure of protein: Formed due to twisting of polypeptide chain.The folding is due to…
Q: Consider the second titration. PH 14.0 12.0 10.0 8.0 10 11 7 4 1 9 6.0 4.0 2.0 0.0 0.5 1.0 1.5 2.0…
A: Titration is used for determining the amount of acid in a solution. Sodium hydroxide is added to a…
Q: The pKas of two hypothetical organic acids are given below: ACOOH ----> ACOO- + H+ (pKa = 4.15)…
A: According to Henderson and Hesselbach equation.PH = Pka + log [A-] /[ HA].So if the acid is soluble…
Q: g) Do some research. How does the level of phosphocreatine remain high in muscle cells. Where/how is…
A: Phosphocreatine (PCr) levels in muscle cells are maintained through a process called the creatine…
Q: 22. If 75 mls of 0.02 M HCI is added to 425 mls of 0.5 M glycine buffer at pH 10.4, what is the…
A: Here given that, there is 425 mL of 0.5M glycine buffer at pH 10.4425 mL is equal to 0.425 L…
Q: The tripeptide Glu-Pro-Arg (EPR) which is a product of Lactobacillus casei fermentation of milk was…
A: A peptide is a name assigned to short polymers of amino acids that are less than 50. Tripeptide is…
Q: What are the characteristics of a secondary antibody used in Western blotting? contains a covalently…
A: Western blotting is a laboratory technique used to detect a specific antigen containing protein in…
Q: The compound below, doxorubicin, is a substrate for p-glycoprotein. Cancer cells with a higher…
A: Cancer is mainly caused by the uncontrolled proliferation of cells due to mutation. Doxorubicin is…
Q: Tyrosine came from the Greek word "tyros" which means cheese as it was discovered in cheese by…
A: Tyrosine is a crystalline amino acid with a molecular formula of C9H11NO3. It is a non-essential…
Q: The value of AGO for the conversion of 3-phosphoglycerate to 2-phosphoglycerate (2PG) is +4.40…
A:
Q: For the enthalpy (H) factor to become favorable, the enthalpy of the products should be O Higher…
A: The question is to identify the condition of enthalpy of product with respect to reactants when the…
Q: Please provide explanations and work for each part of the question. If able to keep the same format…
A: Protein structure is a fundamental concept within biochemistry, encompassing the hierarchical…
Q: Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction…
A: The reactions in which the electrons are transferred from one substance to the other substance are…
Q: Discussing the Data - Class Average vs Group 9. Use the % change my group for the unknown a. Square…
A: The following worksheet contains so many questions and many of them are solved. Those unsolved are…
Q: From a kinetics experiment, kcat was determined to be 295sec-1. For the kinetic assay, 0.3mL of a…
A: Let the initial concentration of the enzyme in the reaction mixture be E0E0 = (Volume of enzyme…
Q: Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt…
A: Salt bridges are attractive interactions between two oppositely charged groups. So, more oppositely…
Q: Explain why unfolding or aggregation may occur using changes in entropy and enthalpy of the protein…
A: Adding a small amount of salt into a protein solution can increase the solubility of the protein in…
Trending now
This is a popular solution!
Step by step
Solved in 3 steps
- Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobins.b. Are the mildly thalassemic individuals with Leporehemoglobin homozygotes or heterozygotes for theunusual allele?c. Why might these mildly thalassemic people produce less Lepore hemoglobin than normal adulthemoglobin?Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobinsA) describe in molecular detail how protonation of the histidine side-chain results in hemoglobin's lower affinity for oxygen. b) what value do you expect for the pKa of the histidine side-chain ionizable group?
- 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!)1. In fetal hemoglobin, residue 143 of the beta subunit is a serine rather than the histidine found in adult hemoglobin (see figure on page 9). a) What does this do to the charges in the BPG binding cavity? b) Would you expect this to change the oxygen affinity of fetal hemoglobin, and, if so, in what direction?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 hemoglobin from patients with sickle cell anemia, the hemoglobin ß-chains have a single amino substitution that results in: A) A sticky spot in the hemoglobin causing polymerization O B) A change in the oxygen binding to hemoglobin that causes formation of polymers C) Changes in the interaction between B-chains and x-chains OD) Changes in binding of 2,3-bisphosphoglycerateWhat qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.The α and β subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, in the subunits of hemoglobin, certain residues that are hydrophilic in myoglobin are hydrophobic. Why might this be the case?
- 2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?A team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…