
Concept explainers
(a)
To draw: A diagram showing what a head-antibody-myosin complex might look like at the molecular level.
Introduction:
Antibodies are the Y-shaped proteins which provide immunity to the body by neutralizing antigens such as bacteria and virus. They are also known as immunoglobulins. An antigen is a foreign particle that induces the production of antibodies. These protein structures are the three-dimensional arrangement of atoms in a peptide chain.
(b)
To determine: The reason for the requirement of ATP for the beads to move along the actin fibers.
Introduction:
Adenosine triphosphate (ATP) is the energy currency of the cells that are produced during glucose
(c)
To determine: The reason for the failure of experiment if antibodies used were bound to the part of S1 and, if antibodies were bound to actin.
Introduction:
Myosins are the muscle proteins that carry out the muscle contraction and provide a wide range of motility in humans and other animals. Myosin proteins are known to interact with the actin fibers for motility processes. Antibodies are the Y-shaped proteins which provide immunity to the body by neutralizing antigens such as bacteria ad virus.
(d)
To determine: Why might trypsin attack the specific single peptide bond first rather than other peptide bonds in myosin.
Introduction:
Heavy meromyosin (HMM) and short heavy meromyosin (SHMM) are the two products of the digestion of the meromyosin. Meromyosin proteins can be digested by using trypsin in the process called proteolysis. Meromyosin is a part of the myosin protein These together form the muscle fiber called sacromere.
(e)
To determine: The model (S1 or hinge) that is consistent with the results observed in subpart (d).
Introduction:
The S1 fragment in the myosin acts as a motor domain and is involved in the contraction of the muscle. Hinge region is the region where cleavage with papain separates the immunoglobulin in two portions Fab (antigen-binding) portion and Fc (crystallizable fragment). Thehe region where they get separated known as hinge region.
(f)
To provide: A possible explanation for the increased speed of the beads with increasing myosin density.
Introduction:
The beads that are involved in the bead-antibody-myosin complexes are coated with the myosin and move along with the actin fiber that are associated with the myosin. Myosins are the muscle proteins that carry out the muscle contraction and provide a wide range of motility in humans and other animals.
(g)
To provide: A possible explanation for the plateauing of the speed of the beads at high myosin density.
Introduction:
Myosins are the muscle proteins that carry out the muscle contraction and provide a wide range of motility in humans and other animals. The beads that are involved in the bead-antibody-myosin complexes are coated with the myosin and move along with the actin fiber that are associated with the myosin.
(h)
To determine: The reason why SHMM was still capable of moving beads along the actin fibers.
Introduction:
Short heavy meromyosin (SHMM) and heavy meromyosin (HMM) is a product of digestion of meromyosin by the trypsin enzyme. Meromyosin is part of the myosin protein. Myosin is the muscle protein that along with actin involved in the muscle contraction.
(i)
To provide: A suitable explanation of the protein that remains intact and functional even though the polypeptide backbone has been cleaved and is no longer continuous.
Introduction:
Proteins are the

Want to see the full answer?
Check out a sample textbook solution
Chapter 5 Solutions
Lehninger Principles of Biochemistry
- 2. Which one is the major organic product obtained from the following reaction sequence? HO A OH 1. NaOEt, EtOH 1. LiAlH4 EtO OEt 2. H3O+ 2. H3O+ OH B OH OH C -OH HO -OH OH D E .CO₂Etarrow_forwardwhat is a protein that contains a b-sheet and how does the secondary structure contributes to the overall function of the protein.arrow_forwarddraw and annotate a b-sheet and lable the hydrogen bonding. what is an example that contains the b-sheet and how the secondary structure contributes to the overall function of your example protein.arrow_forward
- Four distinct classes of interactions (inter and intramolecular forces) contribute to a protein's tertiary and quaternary structures. Name the interaction then describe the amino acids that can form this type of interaction. Draw and annotate a diagram of the interaction between two amino acids.arrow_forwardExamine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript. e₁ e3 e4 A B с 1° B' 02 e5 e6 e7 E F Which enzymes catalyze irreversible reactions? ப e ez ☐ ez e4 ☐ ப es 26 5 e7 Which of the enzymes is likely to be the allosteric enzyme that controls the synthesis of G? €2 ез e4 es 26 5 e7arrow_forwardAn allosteric enzyme that follows the concerted model has an allosteric coefficient (T/R) of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. Select the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate concentration, [S]. ㅁㅁㅁ The enzyme would likely follow Michaelis-Menten kinetics. The plot of V versus [S] would be sigmoidal. The enzyme would mostly be in the T form. The plot of V versus [S] would be hyperbolic. The enzyme would be more active.arrow_forward
- Penicillin is hydrolyzed and thereby rendered inactive by penicillinase (also known as ẞ-lactamase), an enzyme present in some penicillin-resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kDa. The amount of penicillin hydrolyzed in 1 minute in a 10.0 mL. solution containing 1.00 x 10 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. Plots of V versus [S] and 1/V versus 1/[S] for these data are shown. Vo (* 10 M minute"¹) 7.0 6.0 5.0 4.0 3.0 20 1.0 0.0 о 10 20 30 1/Vo (* 10 M1 minute) 20 103 90 BO 70 50 [S] (* 100 M) 40 50 60 y=762x+1.46 × 10" [Penicillin] (M) Amount hydrolyzed (uM) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61arrow_forwardConsider the four graphs shown. In each graph, the solid blue curve represents the unmodified allosteric enzyme and the dashed green curve represents the enzyme in the presence of the effector. Identify which graphs correctly illustrate the effect of a negative modifier (allosteric inhibitor) and a positive modifier (allosteric activator) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes for each type of modifier. Negative modifier Reaction velocity - Positive modifier Substrate concentration - Reaction velocity →→→→ Substrate concentration Answer Bankarrow_forwardConsider the reaction: phosphoglucoisomerase Glucose 6-phosphate: glucose 1-phosphate After reactant and product were mixed and allowed to reach at 25 °C, the concentration of each compound at equilibrium was measured: [Glucose 1-phosphate] = 0.01 M [Glucose 6-phosphate] = 0.19 M Calculate Keq and AG°'. Код .0526 Incorrect Answer 7.30 AG°' kJ mol-1 Incorrect Answerarrow_forward
- Classify each phrase as describing kinases, phosphatases, neither, or both. Kinases Phosphatases Neither Both Answer Bank transfer phosphoryl groups to acidic amino acids in eukaryotes may use ATP as a phosphoryl group donor remove phosphoryl groups from proteins catalyze reactions that are the reverse of dephosphorylation reactions regulate the activity of other proteins catalyze phosphorylation reactions PKA as an example turn off signaling pathways triggered by kinasesarrow_forwardConsider the reaction. kp S P kg What effects are produced by an enzyme on the general reaction? AG for the reaction increases. The rate constant for the reverse reaction (kr) increases. The reaction equilibrium is shifted toward the products. The concentration of the reactants is increased. The activation energy for the reaction is lowered. The formation of the transition state is promoted.arrow_forwardThe graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. The mutations are identified as: • The first letter is the one-letter abbreviation for the amino acid being altered. • The number identifies the position of the residue in the primary structure. ⚫ The second letter is the one-letter abbreviation for the amino acid replacing the original one. • Uncat. refers to the estimated rate for the uncatalyzed reaction. Log₁(S-1) Wild type S221A H64A -5 D32A S221A H64A D32A -10 Uncat. How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the…arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON





