1. explain why the substitution of Leu > Val and Arg Lys in protein does not cause a decrease in the biological activity of the enzyme ! 2. explain why the substitution of Ala → Pro and Gly → Val in protein does not cause a decrease in the biological activity of the enzyme !
Q: . Which type of proteins are also known as denatured proteins? A. Primary proteins B. Secondary…
A: Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: Which of the following is not a function of proteins? Select one: a. Structure b. Catalysis c.…
A: Proteins are a class of nitrogenous organic compounds, which are composed of one or more long chains…
Q: 2. Draw the structural formula of the amino acid asparagine that predominates in solution at each of…
A: Asparagine is a polar amino acid. It contains one amide group in its side chain which is not…
Q: 1. If the second amino would the protein sti
A: Answer. Amino acids are compounds containing carbon, hydrogen, oxygen, and nitrogen. They serve as…
Q: Suppose you adjusted the pH of the biotin solution to 4.5 - what effect would that have on the…
A: Biotin is a vitamin which is also called as Vitamin B7. Biotin is a polar compound with it's…
Q: At which position(s) are amino acids limited to those Which amino acid(s) are more commonly found at…
A: Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…
Q: In some cases, a single amino acid substitution can cause a protein to lose its biological activity.…
A: Amino acids are colourless, crystalline solids containing two functional groups- amine and carboxyl.…
Q: The net charge of the dipeptide GD at pH 8.0 is: (pKa ‘s amino terminal is 10, pKa carboxy…
A: Proteins are the building blocks of the body. They are biomacromolecules composed of one or more…
Q: Explain what is meant by the one gene-one polypeptide hypothesis (why was it changed from one…
A: One gene-one polypeptide hypothesis is a theory that each gene is responsible for the synthesis of a…
Q: I need help with question 6
A: Enzymes are proteins which have a fixed shape and structure.When there is a large change in pH,…
Q: 4. Which of the following is an example for group specificity? a) Trypsin hydrolyzing peptide…
A: Group specificity - It implies that the enzyme will catalyze a particular reaction on the function…
Q: . When digesting a complex carbohydrate, water is added and, a simple sugar is obtained through…
A: During digestion the large molecules are broken down into simple molecules like during protein…
Q: One of the nitrogen atoms present in urea came from glutamate. true or false
A: Urea accounts for 80 to 90% of nitrogenous compounds which are excreted through urine. Urea is…
Q: 1. What is the significance of the effect of pH to enzyme activity in relation to the medical…
A: When there is any dysfunction in the body due to the invasion of any foreign particle or pathogen…
Q: I. Normal human blood plasma contains all the amino acids required for the synthesis of body…
A: Blood consists of plasma and solid components i.e., white blood cells (WBC), red blood cells (RBC),…
Q: 1. Why did you use buffer instead of distilled water to dilute the enzyme and the substrate?
A: Note: Since you have posted multiple independent questions in the same request, we will solve the…
Q: 6. What happens to substrate molecules at an enzyme active site? A. They become catalysts. B. They…
A: “Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: Amino acids with non-polar side chains are zwitterions at a. middle pH levels, between the pKa’s of…
A: Amino acids are compounds with an amino group, a carboxyl group, a hydrogen atom, and a variable…
Q: It is impossible for a mixture of amino acids to make one unique type of proteins because, free…
A: Amino acids are the polymers of proteins and these are linked by a peptide bond to form a…
Q: 1. What are enzymes? Describe briefly each class of enzyme according to its function. 2. What are…
A: The process that converts one chemical entity to another chemical entity is called a chemical…
Q: We have talked about the importance of shape in relationship to enzyme function. Describe the 4…
A: The four levels of protein structure are primary, secondary, tertiary, and quaternary. Protein…
Q: The following bond makes bovine pancreatic trypsin inhibitor as one of the stable proteins.…
A: Introduction: Bovine pancreatic trypsin inhibitor (BPTI) binds to trypsin and prevents peptide…
Q: 1. The 3-dimensional conformation of proteins is stable but also dynamic. There are two reasons…
A: The primary structure of a protein — its amino acid sequence — drives the folding and intramolecular…
Q: and s stand (A) Vitamin 012 can be reduced to forms B12, and B12, What is the abbreviationr for? (B)…
A: Vitamins are vital nutrients required for the normal functioning of the body. They act as cofactors…
Q: 8. Match each of the following amino acids with the intermediate needed for its synthesis. (a)…
A: The non-essential amino acids can be synthesized in the body, they need not be supplied in the diet.…
Q: 3. What ingredients are likely to contribute to the largest amount of saturated fat? b. How could…
A: The answer to the above question is given below.
Q: 3. What is the pKa corresponding to the dissociation of the a-carboxylic group? [ Select ] [ Select…
A: Pka is the representation of the strength of an acid. Pka is measured by taking negative log of Ka,…
Q: 6. An allosteric enzyme has which of the following properties? 1. It can only operate in an acidic…
A: Allosteric enzymes are the enzymes that changes their conformation according to the binding of…
Q: 1. Write the reversible reactions with its corresponding enzymes of Dehydration via Hydrolysis…
A: Biomolecules are the biological molecules that are present inside the living organisms. These…
Q: 1. The pka of an acid is partly dependent on the environment of the acid. What will be the effect of…
A: According to the Henderson-Hasselbalch equation, which defines the relationship between the…
Q: Which amino acid(s) are more commonly found at the At which position(s) are amino acids limited to…
A: Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…
Q: The pKa of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH…
A: All amino acids contain atleast two ionizable groups- the alpha-amino group and the alpha-carboxylic…
Q: 1. If the Km of an enzyme for substrate A is 1 x 106 and for substrate B, is 4 x 10°, it means a.…
A: The Michaelis constant, Km, varies considerably from one enzyme to another, and also with a…
Q: Amino acid residues commonly found in the middle of B turn are: a. Pro and Gly. O b. two Cys. c.…
A: The most commonly amino acid residues found in the middle of beta turn is proline and glycine. It…
Q: 1. The substrates bond to the enzyme's product 2. A structure known as an "enzyme-substrate complex"…
A: These are multiple choice questions.
Q: In the chemical mechanism of chymotrypsin, the group that acts as a general base in the deacylation…
A: Hi! Thanks for your question. As you have posted multiple questions and have not mentioned which one…
Q: 4. The enzyme trypsin is sold as a dietary enzyme supplement Explain what happens to trypsin that is…
A: Trypsin refers to an enzyme that belongs to the PA clan superfamily of proteases. It is a serine…
Q: Explain why sucrose is non reducing sugar
A: The carbohydrates that are capable of causing the reduction of other substances without being…
Q: 3. How does changes in enzymatic factors affect the native conformation of enzymes? What happens to…
A: Enzymes are proteins which act as bio catalysts. They are heat labile and water soluble. Since…
Q: What does phosphorylation do to a pl of amino acid? 1. The pl value is not changed. 2. pl is…
A: Explanation: Each amino acid has a specific pI value i.e the isoelectric point of that amino acid.…
Q: If the pH of pepsin has reached 8.5, explain what could happen to the structure and function of the…
A: Pepsin is an aspartic protease and its activity is directly dependent on the pH of the solution…
Q: How do the ligand (substrate) and the protein/enzyme predominantly interact? O sigma bonds O…
A: Note: We are authorized to answer one question at a time since you have not mentioned which question…
Q: 9. Describe how synthesis of fatty acids is a spontaneous reaction based on coupling to favorable…
A: Hello. Since you have posted multiple questions, we will solve the first question for you. If you…
Q: 8. Fat-soluble vitamins. Name the compound shown below. Explain: a. Which compound is the precursor…
A: A body requires certain organic molecules in small quantities in its diet to maintain proper growth…
Q: 1. Look up the mutation associated with Hemoglobin Hammersmith. A.) Identify the amino acid changed…
A: Hemoglobin is a protein found in the RBCs which is responsible for the transport of oxygen from…
Q: 6-An example of a hydrolysis reaction is * a.dipeptide + H20 → amino acid + amino acid O b.…
A: Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: Which of the following are general properties of active sites? MARK ALL THAT APPLY. Group of…
A: Those substances that elevate the chemical reactions without undergoing any change to themselves…
Q: Amino acid side chains are very important for their function in protein. Sometimes mutations can…
A:
Q: 8. Enzyme activity can be registered by one form of covalent modification called phosphorylation.…
A: Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: Why does enzyme activity decrease because of pH changes? A. Disruption of hydrogen-bonding…
A: Enzymes are biological catalysts that accelerate chemical reactions within the cells. Proteins…
Step by step
Solved in 3 steps
- In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation1. Describe the two ways by which the activity of an enzyme can be inhibited.
- 1. There are two major categories of enzyme, inhibition, name, and describe them.  1a. Reverse inhibition can be overcome to allow the enzyme to resume is Catley activities. Describe how reversible inhibition can occur and how it can be over come.5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
- 1. Please identify the substrate and type of reaction, and explain how these reactions work for the following two enzymes Two enzymes: succinate dehydrogenase and L-amino acid reductase1. The antibiotics puromycin and erythromycin are known inhibitors of protein synthesis. (a) Which part of the protein synthesis is affected by each antibiotic? (b) What could be the reason why one of them is more effective than the other one when they are given in the same dose?1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sure
- 6. Why would the lack of lactase cause Carol so much distress? Where would the undigested lactose travel from the small intestine. a) what could the production of gas from the breakdown of sugar. 7) Are enzymes only important for digestion, as is the case with lactase? 8. Why would it be important to regulate the function of an enzyme at all? Please read the reading, and then answer the questions.8. Enzyme activity can be registered by one form of covalent modification called phosphorylation. True or false 16. The ionized of all amino acids at pH (7.4) has a net charge of zero. True or false 17. Like beans, eggs would be most likely to be deficient in at least one of essential amino acid. True or false8. A dipeptide T, obtained from the breakdown of an enzyme found in the human body, is made up of Amino Acids R and S. (a) Classify Amino Acids R and S as an acidic amino acid or a basic amino acid. (b) Name Bond Q. (c) State any ONE type of protein that could be found in human body. (2%) (1%) (1%)