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 solutionChapter 5 Solutions
Lehninger Principles of Biochemistry
- a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark) b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark) c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)arrow_forwarda) What are the differences between the Direct & Indirect Immunofluorescence Assays? b) What are the advantages of the Indirect Immunofluorescence Assays? c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?arrow_forwardCalculate the number of ATP produced from oxidation of 1 molecule of glucosearrow_forward
- Example 1: 1. Suppose an enzyme (MW = 5,000 g/mole) has a concentration of 0.05 mg/L. If the kcat is 1 x 10 s, what is the theoretical maximum reaction velocity for the enzyme? A) 1050 µM/s. B) 100 µM/s. C) 150 μM/s. D) 105 μM/s.arrow_forwardIn 1956, E. P. Kennedy and S. B. Weiss published their study of membrane lipid phosphatidylcholine (lecithin) synthesis in rat liver. Their hypothesis was that phosphocholine joined with some cellular component to yield lecithin. In an earlier experiment, incubating 32 P-labeled phosphocholine at physiological temperature (37 °C) with broken cells from rat liver yielded labeled lecithin. This became their assay for the enzymes involved in lecithin synthesis. Determine the optimal pH for this enzyme and characterize the enzyme activity at different pH values. -O-P-O-CH2-CH₁₂-N(CH3)3 Phosphocholine H₂C-O-C-R HC-O-C-R2 + + + Cell fraction + ? HC-O-P-O-CH₁₂-CH₂-N(CH), O Phosphatidylcholine The researchers then centrifuged the broken cell preparation to separate the membranes from the soluble proteins. They tested three preparations: whole extract, membranes, and soluble proteins. Table 1 summarizes the results. Table 1: Cell fraction requirement for incorporation of 32p-phosphocholine into…arrow_forwardResearchers isolated an unknown substance, X, from rabbit muscle. They determined its structure from the following observations and experiments. (a) Qualitative analysis showed that X was composed entirely of C, H, and O. A weighed sample of X was completely oxidized and the H2O and CO2 produced were measured. This quantitative analysis revealed that X contained 40.00% C, 6.71% H, and 53.29% O by weight. (b) The molecular mass of X, as determined by mass spectrometry, was 90.00 atomic mass units (u). (c) Infrared spectroscopy showed that X contained one double bond. (d) X dissolved readily in water, and the solution demonstrated optical activity when tested in a polarimeter. (e) The aqueous solution of X is acidic. What is the empirical formula of X?arrow_forward
- Show work. don't give Ai generated solution....give correct solutionarrow_forwardBiochemistry What is the process of "transamination" in either the muscles or the liver, that involves keto acid or glutamic acid? Please explain how the steps work. Thank you!arrow_forwardBiochemistry Please help. Thank you What is the importance of glutamic acid in the metabolism of nitrogen from amino acids? (we know therole; it’s used to remove the nitrogen from amino acids so that the remaining carbon skeleton can bebroken down by the “usual” pathways, but what is the important, unique role that only glutamicacid/glutamate can do?)arrow_forward
- Biochemistry Please help. Thank you When carbamyl phosphate is joined to L-ornathine, where does the energy for the reaction come from?arrow_forwardBiochemistry Question Please help. Thank you What is the function of glutamate dehydrogenase?arrow_forwardBiochemistry Question Please help. Thank you How and why does a high protein diet affect the enzymes of the urea cycle?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