Concept explainers
(a)
Interpretation:
The amino acid alternation in the upper panel of graph A must be determined.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(b)
Interpretation:
The affect of mutation in colipase enzyme should be determined.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(c)
Interpretation:
The amino acid substitution in the lower panel of graph A must be determined.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(d)
Interpretation:
The effect of above substitution on the ability of colipase to bind the lipase to the lipid particle must be determined.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(e)
Interpretation:
The effect of the L16A mutation on lipase activity should be determined by analyzing the graph B.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(f)
Interpretation:
The lipase-binding and activation properties of the colipase enzyme must be determined.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
(g)
Interpretation:
The effect of the Y55A mutation on lipase activity must be determined.
Concept introduction:
The fatty acids are degraded in a sequential manner, that is two carbon units at the carboxyl end of the molecule are removed in each step. The process of beta-oxidation of fatty acids degrades the fatty acids. The process of fatty acid synthesis is a stepwise process, which occurs by the addition of two-carbon units. These carbon units are provided by the acetyl-CoA, derived from glucose oxidation.
Want to see the full answer?
Check out a sample textbook solution
Chapter 22 Solutions
Biochemistry
- Inducers and Inhibitors of AEP. Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…arrow_forwardproteins. Which of the following will tell you whether a protein would be found in the lumen of the ER? A. You run a hydropathy plot an look for hydrophobic peaks that span 20-30 amino acids B. You isolate microsomes and see whether the proteins are inserted into the membrane of the microsome C. You run a hydropathy plot an look for a lack of hydrophobic peaks that span 20-30 amino acids O D. You do in vitro translation of each protein in the presence or absence of microsomes and look to see whether there is a size change in the presence of microsomes.arrow_forwardPlease help me with this question. How many amino acid residues are in the heavy and light chains of the Fab fragment, and how many amino acid residues are in lysozyme?arrow_forward
- SIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Polymerase with H2N-...GMMTVPPKKKRVGMMTV...-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? What is the receptor of the signal sequence? What is the transport complex for this protein?arrow_forwardI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4arrow_forwardBiotransformation. Explain the process of enzyme induction. What are the benefits or down-falls of this process.arrow_forward
- Using the biosynthesis of aminolevulinate (ALA) as an example, describe at least two techniques that can be used to elucidate detail of a biosynthetic pathway. Please keep brief - 5 sentences/dot points max.arrow_forwardILLUSTRATIONS For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: . . a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none E. Mitochondrion H₂N-MTS ITS* "Internal targeting sequence that has no cleavage site -COOH SALEarrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Catalase with H2N-...KERINGKERIANGEKSAMSKL-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? (specify the compartment) What is the name of the specific receptor of this polypeptide? The receptor may also have what alternative function?arrow_forward
- TPA protein function. Use at least two sentences to describe the function of the TPA protein.arrow_forwardtopic: Bradford AssayThere are numerous methods of protein determination in use, but this module focuses on the Bradford assay.The Bradford assay is a dye-binding method that employs Coomassie Brilliant Blue G-250, whose structureis shown in Figure 2.3.4.1. Coomassie Brilliant Blue G-250 is a dye that interacts with proteins throughhydrophobic and electrostatic interactions. What are the identities and functions of the components of the Bradford reagent in protein contentdetermination?arrow_forwardSmall molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals 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 Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON