A mutation that changes an alanine residue in a protein to an isoelectric, lead to a loss of activity. Activity is regained when a further mutation at the same site changes isoleucine to a glycine. Why?
Q: Do you think the protein that binds to miltefosine would also bind to a triacylglycerol molecule?…
A: Protein binding enhances antimicrobial activity, eliminates drug delaying, and restricts tissue…
Q: How can the phosphorylation of a protein result in conformational changes?
A: Phosphorylation generally alters the structural as well as functionality of protein. It alters the…
Q: Which of the following molecules do NOT contribute atoms to purine synthesis? a. Glutamine b.…
A: Purines are nucleotide bases attached to 5 carbon containing sugar molecules. Adenine and guanine…
Q: Insulin, a hormone release in large part due to carbohydrate consumption and subsequent…
A: Insulin is an essential hormone produced by beta cells of pancreatic islets. The insulin controls…
Q: What characteristics of a binding site determine its affinity for a ligand?
A: The binding site is a region where the upcoming molecule like any ligand/substrate (smaller in size)…
Q: What happens to the activity of an allosteric enzyme if an allosteric inhibitor binds the alloster…
A: Allosteric mode of inhibition is also called non-competitive inhibition where an inhibitor…
Q: Three amino acids that donate amine groups for the purine biosynthesis are a) Glycine, glutamine,…
A: Purines are heterocyclic aromatic compound of carbon and nitrogen and forms nucleotides that in turn…
Q: How does the regulation of protein activity by covalent modulation differ from that by allosteric…
A: The binding of the ions or other molecules to protein results in changes of the conformation of…
Q: Which one of the following statements about the molecular structure of phosphatidylcholine is TRUE?…
A: Phospholipids are a class of lipid molecule that is the most important component of all cell…
Q: Explain Specificity of phospholipases.
A: Phospholipases: An enzyme that hydrolyzes phospholipids into fatty acids and other…
Q: Which of the following amino acids are involved in O-glycosylation linkage? O Tyrosine O Asparagine…
A: O linked glycosylation is a type of post translational modification of polypeptides. It come under…
Q: How do neurodegenerative diseases such as Alzheimer's and Parkinson's disease relate to the concept…
A: Introduction :- The progressive loss of structure or function of neurons, known as…
Q: Describe one function of prostaglandins.
A: The prostaglandins are a group of lipid molecules that are produced near the damaged tissues or at…
Q: H,N NH, NH H;N он
A: Trypsin is a serine protease that cleaves the carboxyl-terminal of arginine /lysine and the amino…
Q: What characterizes the C5 amino acids? These amino acids are converted to glutamate then deaminated…
A: Introduction: Amino acids are compounds that contain an amino group, a carboxyl group, and a side…
Q: Individuals with phenylketonuria must avoid dietary phenylalanine because they are unable to convert…
A: Phenylketonuria eventually leads to an accumulation of phenylketonuria, which can cause mental…
Q: Caffeine is an inhibitor of cyclic AMP phosphodiesterase. How would drink- ing several cups of…
A: Lipid metabolisms is the synthesis and degradation of lipids in cells, involving the breakdown or…
Q: What is cohesins
A: A cell consists of a cell organelle, proteins, carbohydrates, nucleic acids, receptors, etc. Each…
Q: Is the formation of the acyl-enzyme complex a unimolecular (SN1) or biomolecular(SN2) reaction?
A: The most significant difference between a ketone/aldehyde and a carboxylic acid derivative is that…
Q: A protease is an enzyme that catalyzes the hydrolysis of the peptide bonds of target proteins. How…
A: A peptide bond is an amide type of covalent chemical bond linking two consecutive alpha amino acids…
Q: A mutation that changes an alanine residue in the interior of a protein to valine is found to lead…
A: Valine : It is an aliphatic and extremely hydrophobic essential amino acid in humans related to…
Q: What type of interactions can glutamic acid participate in that are not possible for glutamine?…
A: In a biochemical context, the amino acids glutamine and glutamic acid are strongly connected.…
Q: A mutation that changes an alanine residue in a protein to an isoleucine leads to a loss of…
A: The protein folding property of protein makes a major impact on the functioning of amino acids. The…
Q: What is the purpose of having ACP as a distinct activating group for fatty-acid synthesis?
A: Acyl carrier protein (ACP) is an essential part of multienzyme complex known as fatty acid synthase…
Q: If only a few (two or three) amino acid residues are involved in enzyme function, state at two…
A: Enzymes are protein polymers that participate in the biological reactions and act as biological…
Q: What enzyme(s) control the total levels of cGMP in a cell? Is guanylyl cyclase one of the enzymes?
A: Cyclic GMP or cGMP is a second messenger molecule during the process of signal transduction.
Q: Is the statement "elongation is the process of introducing double bond in fatty acid", correct?
A: Fatty acid Elongation is the process in which to make fatty acids longer than 16 carbons occurs in…
Q: Glycoproteins are involved in what kinds of functions? Give at least three examples, each with a…
A: Glycoproteins : Proteins which contain glycan covalently attached to amino-acid side chain.…
Q: Must the amino acid residues in the active site be near each other along the polypeptide chain?…
A: The polypeptide chain is considered as the long sequence of amino acids, which exhibits amino acid…
Q: Which of the following statements is NOT TRUE about tyrosine? O It is an essential amino acid. O It…
A: All living organisms are made up of hundreds of amino acids. These are the polymers that synthesize…
Q: Which of the following amino acid residues would not provide a side chain for acid- base catalysis…
A: Introduction: Nearly one-third of all known enzymes require metal ions for the catalytic activity…
Q: Acid hydrolysis of polypeptides may lead to complete destruction of tyrosine residues.
A: Proteins and peptides are macromolecules made up of covalently bonded amino acid residues in linear…
Q: List some of the functions prostaglandins serve in the body.
A: Prostaglandins are lipids made from eicosanoids. They have hormone-like effects in humans and are…
Q: What is the percent ionization of these amino acids? 1. Aspartame at pH 5.4 2. Glutamate at pH 11.8…
A: Since we are entitled to answer up to 3 sub-parts, we’ll answer the first 3 as you have not…
Q: ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine…
A: Given: ATP synthase is the protein that catalyzes the formation of the energy storage molecule…
Q: Which of the following is NOT a steroid molecule?
A: Testosterone is a primary sex hormone and anabolic steroid in males. Estrogen is one of the sex…
Q: why is ATP preferred to other forms like GTP, CTP, TTP?
A: ATP is a bio-synthetically derived molecule that has multiple biochemical functions to do. ATP is…
Q: On the given choices what is not part of the multi-enzyme complex of fatty acid synthase?
A: Multi-enzyme complex fatty acid synthase: This is a multi-enzyme complex encoded by the FASN gene…
Q: Describe the role of feedback inhibition in controlling amino acid synthesis
A: Amino acids are the basic units that makeup proteins. Amino acids are comprised of carbon, hydrogen,…
Q: In a particular enzyme,an alanine residue is located in a cleft where the substrate bonds.A mutation…
A: Introduction: The functional segment of hereditary material that mainly codes for the proteins is a…
Q: Saponification is a reaction in which a. triacylglycerols are incorporated into lipoproteins b.…
A: Saponification is considered as the process of formation of a soap molecule from lipid, oil, or fat.…
Q: c) Jean-François is studying a specific protein in a research laboratory. he observed that this…
A: Proteins are very senstive to the change in pH as they are functional at a narrow pH range. The…
Q: What is the binding between two amino acids called?
A: Protein is a polymer formed from amino acid joined by peptide bond. It is abundantly found in the…
Q: Nucleotides play a variety of roles in the cell. Give an example of a nucleotide that acts in each…
A: Note: Since you have posted a question with multiple subparts, we will solve the first three…
Q: What function does ATP play in amino acid activation?
A: In a process catalyzed by a Tran-activating enzyme, each Tran molecule binds to a particular amino…
Q: What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of…
A: Chymotrypsin is a proteolytic enzyme.
Q: Glycine is an amino acid whose side group does not participate in any of the types of side group…
A: Every amino acid joined to a different chemical group at the site termed its side chain. By…
A mutation that changes an alanine residue in a protein to an isoelectric, lead to a loss of activity. Activity is regained when a further mutation at the same site changes isoleucine to a glycine. Why?
Trending now
This is a popular solution!
Step by step
Solved in 3 steps
- Which of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation stateIf D-glyceraldehyde-3-phosphate (DGAP) is dissolved in water, 96% of it will form dihydroxy- acetonephosphate (DHAP). Which of the following will triose phosphate isomerase do? a)Shift the balance to 100% DHAP b)Shift the balance to 0% DHAP c)Shift the balance to 50 DGAP : 50 DHAP d)Catalyze the peptide bond breaking e)Make the reaction fasterIn the context of protein synthesis, what is meant by an activated amino acid?
- Explain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting? (Keep your answer to at least a paragraph)If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work? Do not just say yes or no. Give a short explanation for this hypothetical situation.Can an amino acid be both glucogenic and ketogenic? Explain why or why not.
- Draw a phosphorylated tyrosine molecule at physiological pH. Assume that the phosphate group is deprotonated and has a charge of -2. Would the carboxylic acid group of the phosphorylated tyrosine have a lower or higher pKa than that of unmodified tyrosine? Explain.Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…Acetylcholine is inactivated by the enzyme acetylcholinesterase. Which amino acid residue's side chain plays an important role as an acid-base catalyst in the enzyme's mechanism of action? O Glycine O Lysine Histidine Alanine O Asparagine
- Individuals with phenylketonuria must avoid dietary phenylalanine because they are unable to convert phenylalanine to tyrosine. Look up this condition and find out what happens if phenylalanine accumulates in the body. Would you advise a person with phenylketonuria to consume foods sweetened with aspartame? Why or why not?Draw the structure of the α-keto acid formed by the transamination of each amino acid: (a) tyrosine; (b) asparagine.A mutation that changes an alanine to a leucine in the nucleus of a protein leads to a less active one protein. However, the protein can be made active again by introducing another mutation into anotherpart of the protein where phenylalanine is replaced by alanine. How can it be thought of this othermutation leads to the activity being recovered?