A) llustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?
Q: Sickle cell anemia is caused by a point mutation in the β-globin chain of hemoglobin. Glutamic acid…
A: Introduction : Haemoglobin is a tetrameric proteinmade up of 2 alpha subunits and 2 beta subunits…
Q: Consider olive oil, an oil with a high percentage of fat derived from oleic acid (otherwise known as…
A: When the two hydrogen atoms of the fatty acids which adjoin the double bond are in the same chain,…
Q: Hemoglobin is the oxygen carrier in the blood. What is the effect of each of the following…
A: Hemoglobin is considered a globulin protein in the red blood cells, It plays a significant role in…
Q: Methylation. Amino acid decarboxylation. A Claisen reaction. Ketoacid decarboxylation. Aldehyde…
A: Methylation It is the most common but minor pathway as that of sulfonation. The cofactor used in…
Q: Which out of the following amino acids carries a net positive charge at the physilo PH: A) Non of…
A: Amino acids Proteins are the polymers of nitrogenous compounds called amino acids. Each amino acid…
Q: Use the pka values, calculate the isoelectric point (pl) of the following amino acids. a) Leucine b)…
A:
Q: Which of the following amino acid residues would not provide a side chain for acid-base catalysis at…
A: Amino acids are the building blocks of proteins, which are essential to the structure and function…
Q: "The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which…
A: Given: The native structure of hemoglobin (HB) comprises two α and two β subunits, each of which…
Q: Consider the following peptide: Lys-Tyr-Glu-His-Arg-Ala-Asp-Arg-Glu-Tyr-Lys a) What is the net…
A: The proteins are constituted of twenty naturally occurring amino acids that are connected via…
Q: Congenital sucrase-isomaltase deficiency (CSID) is a genetic condition that prevents the metabolism…
A:
Q: What are the donor atoms involved in Aspartame-Cu(II) binding? A) Nitrogen atom of alpha amine group…
A: Aspartame contains two amino acid residues, aspartic acid and phenylalanine, linked by a peptide…
Q: 1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value…
A: Cooperativity or cooperative binding occurs when binding of one molecule influences the affinity of…
Q: In the deoxy state of HB, which of the following does not occur? a) An inter-chain salt bridge…
A: Because hydrogen bonds and salt bridges, or ion-pair bonds, stabilize the deoxygenated form of…
Q: A) Draw L-histidine. Label all ionizable groups with the appropriate pKa.
A: Introduction: Histidine is one of the 20 amino acids with imidazole ring that is highly basic by…
Q: For each of the following sequences determine if they will most likely form an amphipathic α helix,…
A: Proteins are polymers of amino acids. The sequence of amino acids is governed by the sequences of…
Q: Given the following information, which protein would be most difficult to isolate from protein X…
A: Salting and dialysis are the processes used to isolate proteins. Salting is a purification process…
Q: Amino acid analysis of the peptide angiotensin II shows the presence of eight different amino acids…
A: Trypsin and chymotrypsin are proteolytic enzymes, which help to cleave the peptide bonds from…
Q: A decapeptide was isolated from a thermophilic bacteria. Treatment of this peptide with 2-…
A: Proteins are large biomolecules that compose structural and motor elements of a cell, and also as…
Q: In the peptide Ala – Gly – Val – Phe – Tyr, a carboxylate (-COO-) group would bound in which amino…
A: The four types of biological macromolecules are proteins, nucleic acids, lipids and…
Q: A) describe in molecular detail how protonation of the histidine side-chain results in hemoglobin's…
A: Hemoglobin is the primary protein responsible for the transport of oxygen from lungs to different…
Q: . The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is…
A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…
Q: Consider the Fe(Il) heme center in hemoglobin. Iron is colored orange and dioxygen is colored red.…
A: Introduction - Hemoglobin is a globular , oligomeric protein made up of heme and globin. Hemoglobin…
Q: After being stabilized with supplemental oxygen, a blood transfusion, and medication to help with…
A: Hydroxyurea: It is a class of antimetabolites. This class of drug is used to treat cancer. It is a…
Q: The steps involved in the T→ R transition in when oxygen binds to hemoglobin are outlined below.…
A: The correct order of the steps involved in the T → R transition in hemoglobin when oxygen binds is…
Q: Hemoglobin from different species can have different numbers of subunits. Let's consider three…
A: Hemoglobin (Hb) is the oxygen transport protein found in most vertebrates. Hb in nature exhibits…
Q: In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed…
A: Amino acid residues are linked together to form long chains called polypeptides. A polypeptide folds…
Q: A decrease in blood pH causes the histidine side chain of Hb to become _____ favoring the _____…
A: A protein present in the erythrocytes that transports oxygen from the lungs to the cells and…
Q: What are the sources of iron and factors affecting iron absorption ?
A: Iron and its sources in diet: Iron is an important constituent of Red Blood Cells (RBCs) in our…
Q: One sample of the globular protein peroxidase is hydrolyzed by heating with 6 M HC1. A second…
A: Denaturation is the process of loss of native conformation of the proteins. The agents for…
Q: This problem concerns a "typical" tyrosine residue found on the surface of a globular protein. a)…
A: The side chain of tyrosine is ionizable. It has a pKa of 10.1. An ionizable group exists…
Q: A seven-residue peptide was found to have an amino acid composition including glu, val, Lys, met,…
A: phenyl thiohydantoin (PTH)- amino acid derivative The sequence of amino acid for heptapeptide…
Q: An oligopeptide has the following amino acid sequence:…
A: Amino acids are the monomeric unit to form polypeptides. There are 20 different amino acids that…
Q: A heptapeptide was found to have an amino acid composition of Asp, Leu, Lys, 2 Met, Phe and Tyr. (a)…
A: Proteins are important biomolecules in that it plays an important role in many biological functions.…
Q: What qualitative effect would you expect each of the following to have on the Pgp of hemoglobin? (a)…
A: The partial pressure of oxygen in the blood at which the haemoglobin is 50 percent saturated,…
Q: In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a…
A: Hemoglobin is a protein present in the red blood cell. The hemoglobin function is to transport the…
Q: 1. The shape of hemoglobin binding curves is: hyperbolic or sigmoidal 2. a) Based on the binding…
A: Note: As per the guidelines, i could solve only the first three subparts of the question. Please re…
Q: The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2)…
A: The activity of molecule 2,3 phosphoglycerate (BPG) is important to obtain stabilized structure of…
Q: A) Upon entering the body, CH3H9+ reacts with cysteine to form a molecule that is able to pass…
A: Introduction Amino acids are molecules that combine to form proteins. Amino acids and proteins are…
Q: 6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group…
A: Protein modification - Major types of proteins modifications are phosphorylation, acetylation and…
Q: a) Electrospray ionization of this small protein typically results in major charge states of +8, +9,…
A: Mass of ubiquitin = 8560 Da. In proteins and peptides, mass spectrum comprises of series of peaks,…
Q: Patients suffering from sickle cell anemia have a mutation in the gene that codes for one of the…
A: Sickle cell anaemia is an inherited blood disorder characterised by misshapen and rigid red blood…
Q: Which of the following statements about aromatic amino acids is correct? (a) All are strongly…
A: Organic substances known as amino acids include both amino and carboxylic acid functional groups.…
Q: Which step is catalyzed by the enzyme responsible for the Met 2 mutant? (picture attached) A)…
A: Synthesis of the amino acid methionine involves four genes in Neurospora. Methionine mutants cannot…
Step by step
Solved in 3 steps
- 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.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 oxygenAfter staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
- Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.Which of the following is true A) The disulfide bridges formed by reduction of the sulfhydryl groups on cysteine destabilizes protein tertiary structure. B) The disulfide bridges formed by oxidation of the sulfhydryl groups on cysteine destabilizes protein tertiary structure. C) The disulfide bridges formed by oxidation of the sulfhydryl groups on cysteine stabilizes protein tertiary structure. D) The disulfide bridges formed by reduction of the sulfhydryl groups on cysteine stabilizes protein tertiary structure.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 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.Proline is one of the amino acids in the "special" groups of sidechains. One reason for this is the dramatic impact it can have on secondary structure. a) draw the lewis structure for a tripeptide with the sequence Ala-Pro-Ala b) Proline residues are rarely found in alpha helices - in fact, they are often referred to as helix-disrupting amino acids. Thinking about intermolecular interactions, provide an explanation for why proline might disrupt alpha-helices. c) Proline also has a similar effect on beta-sheets, and is rarely found in the middle of beta sheets. Thinking about noncovalent interactions, provide an explanation for why proline might disrupt beta-sheets.Amino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.
- The peptide cys-leu-glu-ala-cys-lys is at pH 7 in oxidizing conditions. Part a) Draw the peptide's titration curve. Part b) What would the pI of the peptide be around?Below is a list of hypothetical Hemoglobin variants. Circle the name of the variant that is most likely to show an increase in BPG binding. Does such a hypothetical variant cause an increase or decrease in hemoglobin's affinity for oxygen? A. Hb Miami: Leu is substituted with Pro in an alpha helix B. Hb California: Val is substituted with Lys at pH 7.0 C. Hb New york: Tyr is substituted with Met, which disrupts the hydrogen bonding at the a131 interface. D All of the aboveThe 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.