(a)
Interpretation:
The reason as to why the denaturation of protein occurs when they are extracted from membranes into an aqueous buffer is to be stated.
Concept introduction:
Denaturation of protein is the dissociation of the secondary and tertiary structure of proteins. It is possible through a variety of reagents and reaction conditions. The primary structure remains the same after denaturation. The one common example of denaturation is a coagulation of protein.
(b)
Interpretation:
The explanation for the prevention of the denaturation of protein when they are extracted from membranes with detergents is to be stated.
Concept introduction:
Denaturation of protein is the dissociation of the secondary and tertiary structure of proteins. It is possible through a variety of reagents and reaction conditions. The primary structure remains the same after denaturation. The one common example of denaturation is a coagulation of protein.
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Organic Chemistry Study Guide and Solutions
- For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?apKa of 3.3. The amino group of alanine has a p?apKa of 8.8. Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7.arrow_forwardAnswer the following questions on the basis of the free energies of formation at 25°C shown in the table at the top of the next page: (a) Does the peptide bond between alanine and glycine form spontaneously under standard conditions?arrow_forwardThe amino acid (S)-alanine has the physical characteristics listed under the structure. How does the melting point of a racemic mixture of (R)- and (S)-alanine compare to the melting point of (S)-alanine?arrow_forward
- a) 75mL of a 0.2M solution of a tripeptide Ser-Cys-His is adjusted to pH=8.6. The solution is then titrated with 50mL of 0.5M HCl. Calculate the new pH value of the tripeptide solution. (Relevant pKa values are: 2.2, 6.0, 8.3, and 9.6). b) Once you've completed the addition of HCl to the tripeptide in part a you then titrate the solution with 30 mL of 0.6M NaOH. Calculate the final pH value of the tripeptide solution.arrow_forwardFor the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a pK₁ of 3. The amino group of alanine has a pK₂ of 8. Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7. concentration ratio: Incorrect X10-3arrow_forwardQ1. The pKa values of Glutamic acid are 2.2, 4.3 and 9.7. H2N HO. OH (a) Calculate the pH of a glutamic acid solution in which the a-amine group is 80% deprotonated? (show your calculation!) (b) Draw the ionic forms of glutamic acid that exist at the calculated pH.arrow_forward
- The mutated form of hemoglobin (hemoglobin S, or HbS) in sickle-cell anemia results from the replacement of a glutamate residue by a valine residue at position 6 in the ß chain of the protein. Normal hemoglobin is designated HbA. Under conditions of low [O₂], HbS aggregates and distorts the red blood cell into a sickle shape. See image of eight aggregated HbS molecules. Sickled red blood cells are relatively inflexible and may clog capillary beds, causing pain and tissue damage. The sickled red blood cells also have a shorter life span, leading to anemia. Which amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6? arginine phenylalanine Aggregate of HbS molecules lysine leucine alanine Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a B chain ranion located in the interior of the neotain In daaxshamaalahin homauar thic nookat is laastad on the curfona of tha 0arrow_forwardYou are going to be using Isoleucine in a buffer. The pKa of the carboxylate group of Isoleucine is 2.36 If you have a 0.1 M solution of Isoleucine at pH 3.22, what fraction (or percent) of the solution is in the deprotonated (COO- ) form?arrow_forwardgiven a solution of alanine at pH 9.00, draw the structure of the species present in appreciable quantities and calculate the concentration of each of these species.arrow_forward
- (d) Provide one example of each of the following type: () Microwave-assisted synthesis (ü) Sonochemical synthesis organicarrow_forwardAll amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group (average pK, of 2.2). Glutamic acid has an ionizable side chain (R group) with a pK, of about 4.1. One of the possible ionization states of glutamic acid is shown in the image. H₂N-CH-C-OH CH₂ At what pH would this structure of glutamic acid be the predominant ionization state? Consider the ionization state of all three of the functional groups. OH The protonated form of the R group of glutamic acid is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the pK, of the R group and the pH of the solution. 2.6 4.1 1.5 Select the pH values at which the charged form of the R group would predominate. 7.0 11.3arrow_forwardWhat happens : (a) When animal charcoal is added to a solution of methylene blue dye. (b) When aqueous solution of raw sugar is passed over beds of animal charcoal.arrow_forward
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