Concept explainers
(a)
Interpretation:
The dissociation constant of protein and antibody A is to be calculated.
Concept introduction:
The protein is made up of different amino acids. The amino acid is the smallest unit of a protein. The protein may be composed of primary, secondary, tertiary and quarternary structure. The antibody is also a type of protein which is derived by plasma cells and it is used by the immune system of the cells.
Answer to Problem 19P
The dissociation constant of a complex between protein and antibody A is
Explanation of Solution
The dissociation constant is defined as the breaking of larger molecules into its smaller units or it is defined as the ratio of products to the reactants with respect to their stoichiometric number.
The reaction corresponding to the dissociation of PA is given below.
The dissociation constant of the above equation is shown below.
The value of dissociation constant is obtained when half of the complex is dissociated as given below.
This is the concentration of protein which is obtained and the concentration of the complex which is dissociated.
The concentration of antibody A is obtained from the graph shown below.
Figure 1
From the graph above.
Substitute values of
Therefore the dissociation constant the complex between protein and antibody A is
(b)
Interpretation:
The dissociation constant of protein and antibody B is to be calculated.
Concept introduction:
The protein is made up of different amino acids. The amino acid is the smallest unit of a protein. The protein may be composed of primary, secondary, tertiary and quarternary structure. The antibody is also a type of protein which is derived by plasma cells and it is used by the immune system of the cells.
Answer to Problem 19P
The dissociation constant of a complex between protein and antibody B is
Explanation of Solution
The dissociation constant is defined as the breaking of larger molecules into its smaller units or it is defined as the ratio of products to the reactants with respect to their stoichiometric number.
Consider a reaction given below.
The dissociation constant of the above equation is shown below.
The value of dissociation constant is obtained when half of the complex is dissociated as given below.
This is the concentration of protein which is obtained and the concentration of the complex which is dissociated.
The concentration of antibody B is obtained from the graph shown below.
Figure 2
From the graph above, the concentration of the antibody is calculated as follows:
Substitute values of
Therefore the dissociation constant the complex between protein and antibody B is
On comparing, it is found that antibody A and B are identical except for one single amino acid. The reason for the generation of antibody B is through gene mutation which permanentlychanges the DNA sequence of a species. It may be hereditary or acquired mutation. Since in this case only one amino acid changes.
Therefore, the mutation is a point mutationthat generated antibody B.
Want to see more full solutions like this?
Chapter 35 Solutions
Biochemistry (Looseleaf)
- α-Pinene (4) is synthesized enzymatically from nerol pyrophosphate 1. Drawn an arrow-pushing mechanism from 1 to 2 to 3 to 4; add explicit hydrogens to clarify, if needed.arrow_forwardA reverse phase column chromatography separates proteins according to their polarity. Which pentapeptide will be eluted FIRST when chromatographed at pH 7 using a reverse phase column such as a C-18 column? Peptide Sequence (from N-terminal to C-terminal) AKGED GAAVF ALLLI MCYAG GAAVF MCYAG ALLLI AKGEDarrow_forwardMelting of three DNA samples with varying lengths was monitored by increase of ultraviolet light absorbance at 260 nm. Which is the shortest DNA? A B Carrow_forward
- Select the CORRECT description of the peptide bond. The peptide bond can freely rotate around the peptide bond. The peptide bond is non-polar, hydrophobic and does not have a dipole. The peptide bond is most stable in the cis configuration. The peptide bond is rigid and planar. The peptide bond has a mix of single and double bond characters. The peptide bond is most stable in the trans configuration.arrow_forwardBelow is a fractional saturation curve for O2 binding to adult hemoglobin. Assume that curve Y represents a system at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve Z represents a system that ___________________ Curve Z: is at pH 7.4 with a higher than normal physiological level of 2,3-BPG. is at pH 7.4 with a normal physiological level of 2,3-BPG but with a decreased level of CO2. has a higher pH with a normal physiological level of 2,3-BPG. has a higher pH with a lower than physiological level of 2,3-BPG.arrow_forwardWhich is a homotropic positive effector of aspartate transcarbamoylase (ATCase)? oxygen CTP aspartate ATParrow_forward
- The reaction scheme shows the mechanism of chymotrypsin-catalyzed peptide hydrolysis. Select ALL CORRECT statements regarding the chymotrypsin mechanism. Serine is the nucleophile in the step 3. Histidine is a general base in the step 2. Carbonyl carbon is the electrophile in the step 3. Histidine is a general acid in the step 4. Carbonyl carbon is the nucleophile in the step 3. This is an example of covalent catalysis. Aspartate is the electrophile in the step 3. Histidine is the nucleophile in the step 3.arrow_forwardThe following shows a protein with mostly beta sheet secondary structures. Which force stabilizes the beta sheet secondary structure of proteins? hydrophobic interactions between nonpolar amino acid side chains within the protein. electrostatic interactions between lysine and aspartic acid residues within the protein. hydrogen bonding between hydrogen bond donors and hydrogen bond acceptors of the peptide backbone. covalent disulfide linkages between cysteine residues within the protein.arrow_forwardThe Lineweaver-Burk plot was obtained when enzyme inhibition study was done in the absence and presence of 0.50 mM inhibitor. Answer the following questions using correct units and significant figures: (a) What is the mode of inhibition, competitive, uncompetitive, mixed, or noncompetitive? Explain your answer. (b) What can you say about the finding site for the inhibitor in relation to the active site of the enzyme? Explain your answer. (c) Calculate the Km and Vmax in the absence of inhibitor. (d) Calculate the Km and Vmax in the presence of 0.50 mM inhibitor. (e) Calculate the KI of the inhibitor using the given equations for reversible inhibition. Which has a higher affinity, the substrate or the inhibitor? How can you tell?arrow_forward
- Which peptide sequence is most likely to be found in the interior portion of a water-soluble globular protein? GGDGEMG DSKSTEG GAIVLWL IVAKSLIarrow_forwardThe following shows a reaction coordinate diagram. Choose a CORRECT statement explaining the diagram. The size of C decreases in the presence of an enzyme. B indicates the activation energy of the reaction in the presence of an enzyme. C indicates the activation energy of the reaction in the presence of an enzyme. A is related to the equilibrium constant of the reaction in the absence of an enzyme.arrow_forwardSelect ALL correct statements regarding myoglobin and hemoglobin. Statements: Myoglobin has a higher affinity for oxygen than hemoglobin does. Both myoglobin and hemoglobin contain mostly alpha-helical structures. Myoglobin has one binding site for 2,3-BPG. Hemoglobin is a tetramer, each of which binds one heme group. In both myoglobin and hemoglobin, iron ions (Fe2+) bind directly to oxygen. Myoglobin is a tetrameric protein. Hemoglobin exhibits cooperative binding with oxygen. Myoglobin does not. Hydrogen ion, carbon dioxide, and 2,3-BPG are negative allosteric effectors of oxygen binding to hemoglobin. Myoglobin has a lower P50 for oxygen than hemoglobin does. Hemoglobin has a higher affinity for oxygen than myoglobin does. Both myoglobin and hemoglobin exhibit cooperative binding to oxygen.arrow_forward
- Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning