QUESTION 20 How many amino acid side chains in this peptide are capable of absorbing light at 280nm? CON O 4 0 3 01 O none
Q: Question 40 How are proteins different from one another they always contain different numbers of…
A: Proteins are biopolymers made of amino acids joined by peptide bond. Proteins are the structural and…
Q: Question 22: which of the following secondary structures would you expect to find on the surface of…
A: Proteins are unbranched polymers constructed from 22 standard α-amino acids. They have four levels…
Q: Question 6 Is LC8 an enzyme? Why or why not?
A: LC8 performs several functions in the cell as a motor protein dynein component as well as in the…
Q: QUESTION 39 Which peptide has a greater absorbance at 280 nm? Glu-Leu-Gln-Phe-Thr-Leu-Asp-Gly-Tyr O…
A: Biological macromolecules are those large molecules that are necessary for the survival and growth…
Q: Question 31 Lipids, aside from their structural and energy storage functions, are also able to…
A: Lipids are composed of hydrocarbons and for this reason they are hydrophobic in nature. Different…
Q: Question 16 Which of the following statements is NOT true regarding the comparison of the…
A: Answer - option C.Each is stabilized by inter chain hydrogen bonds.
Q: QUESTION 4 Which one of the following compounds contains these chemical bonds and groups: fatty…
A: Phospholipids are lipid molecules that consist of hydrophilic phosphate heads and hydrophobic lipid…
Q: QUESTION 5 Which of the following amino acids is most unlikely to be present in a beta sheet?…
A: In the β-pleated sheet, the sheet are formed due to hydrogen bonding between atoms on the peptide…
Q: Question 4 a-D-galactose from B-D-glucose can be differentiated using which method of analysis? O…
A: Alpha - D - Glucose and Beta - D - Glucose are the two cyclic hemiacetal forms of D - Glucose, which…
Q: QUESTION 1 Regarding the following peptide sequence, which of the following statements is FALSE?…
A: *Note: Since you have asked multiple question, we will solve the first question for you. If you want…
Q: QUESTION 6 Disulfide bonds stabilize structures of proteins Tertiary and Quaternary primary…
A: Quaternary structure- Formed by more than 1 protein chains/subunits. Disulfide bond formed involves…
Q: Question 4. You must cleave the following peptide into smaller fragments. How many peptides would…
A: Proteins are complex molecules formed by the polymerization of amino acid residues. Amino acids are…
Q: Question 6. The solubility of globular proteins, when dissolved in water, is influenced by the…
A: Globular proteins are the folded proteins that consists of hydrophilic aminoacids on the surface and…
Q: Question 5 The highest level of protein structure represented here is quaternary O primary O…
A: Proteins are polymers of amino acids. There are four levels of protein structure - Primary…
Q: Question 17 Which of the following are true regarding proteins? Select all that apply. O the amino…
A: 2,3,6. Mild increase in temperature usually increases or maybe doubles the function of enzymes but…
Q: QUESTION 14 The pks of histidine for a-carboxylate =1.8, for a-amino =9.33; and for imidazole (side…
A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…
Q: QUESTION 8 Amino Acids that carry a positive charge of +1 at pH 7 are (Think about it - don't rush…
A: When many amino acids are joined with each other by a peptide bond they form a…
Q: QUESTION 3 Imagine that a proline is present at position 4 in an alpha helical structure, the number…
A: The α-helix is a rigid, rod like structure that forms when a polypeptide chain twists into a helical…
Q: Question 21 Which of the following is likely the reduction potential for CuB in Complex IV? 0.99 V…
A: Electrons move from low reduction potential molecule to high reduction potential molecule. Complex-I…
Q: Question 6 What kinds of bonds do lipase break in order to release fatty acids from…
A: Lipids are hydrocarbons that are made up of carbon and hydrogen mainly. As they are hydrocarbons, so…
Q: What is the three ketter code for each peptide (a) KFYV (b) ERSC (c) PIMF The 3-letter code…
A: Amino acids are the fundamental units of proteins. The amino acids are linked together by means of…
Q: QUESTION 8 Imagine that a proline is present at position 4 in an alpha helical structure, the number…
A: Proline: Has secondary amino group(NH) involved in 5 membered ring structures and 2 bonds formed in…
Q: Question 9 What structural features are true regarding the transmembrane and cytoplasmic domains?…
A:
Q: QUESTION 6 Tertiary structure disulfide linkages occur between which amino acids? O a. cysteine and…
A: Here i discuss about the questions related to the protein structures.
Q: Question 12 What is the net charge of peptide Ala-Gly-Lys-Tyr at a pH of 1.0? O a. 0 Ob. +2 O C. -1…
A: Peptides are the chain of few amino acids joined by the peptide bond. Two amino acids are linked…
Q: Question 3. Which amino acid is most likely to be found in the hydrophobic core of a protein? A.…
A: Please follow step 2 for detailed explanation.
Q: Question #28 Polysaccharides are different from polypeptideș in which of these Ways? A)…
A: Carbohydrates are biomolecules made up of carbon, hydrogen, and oxygen that's why also known as…
Q: Question 12 Starting from glutamine + aspartate + glycine + CO2+ N10-formyl-THF + ribose-5-P: How…
A: The biosynthesis of purine
Q: Imagine you have a mixture of 2 proteins. Protein A is 3x the mass of protein B. Both have net…
A: The Gel electrophoresis works on the migration property of charged species within an electric field,…
Q: QUESTION 10 There are 2 tyrosines, 6 phenylalanines, and 3 tryptophan in bovine protein. The Molar…
A: It is given that bovine protein has 2 tyrosine, 6 phenylalanine, and 3 tryptophan residues present…
Q: QUESTION 7 Which level of protein structure results entirely from hydrogen bonding? O secondary O…
A: the correct option is the : d. both A and D
Q: QUESTION 4 What percent are the following two 20 amino acid peptides similar? MTEKRVQDKAKLIVDEQACT…
A: Answer of the question given below...
Q: QUESTION 3 The speed at which proteins and nucleic acids migrate on an electrophoresis gel has to do…
A: In this technique the samples are loaded into wells at one end of a gel and an electric current is…
Q: PLEASE ANSWERr ASAP
A: GLUT 5 is expressed in small intestine at apical border of enterocytes. It helps in facilitated…
Q: Question 2 Molecular switches govern intracellular signal transduction by switching a protein…
A: The Central Dogma is the process of converting genetic molecules into functional products, in which…
Q: QUESTION 23 Which physical characteristic is not commonly used in protein separation? OA.…
A: As per the guidlines we are supposed to answer only first question posted in case of multiple…
Q: QUESTION 2 The 8th amino acid (assuming its not a proline) in an alpha helix chain will form H-bond…
A: α helix is a secondary conformation of proteins. The amino acids which are joined together through…
Q: QUESTION 10 Carefully analyze the structures of the peptides 1-4 and determine which of the…
A: Amino acids are the monomeric units of proteins or polypeptides. Each amino acid has an amino…
Q: Question 27 ( Which of the following is true of all amino acids? One single codon codes for each…
A: Amino acids are the building blocks for the proteins responsible for the biological functions within…
Q: QUESTION 15 The side chain of would become hydrophobic if its amino group is removed. O tyrosine O…
A: The basic knowledge required to classify an amino acid as a hydrophobhic is it's side chain do not…
Q: GENETICS - help me please
A: Statement 2 "The sequence of amino acid in a polypeptide is specified by ribosomal RNA" is false.…
Q: Question 43 Nucleotide triphosphates and nucleotide diphosphates often form stable complexes with Na…
A: Nucleotide triphosphate is made up of three phosphate groups, 1 deoxyribose sugar and a nitrogenous…
Q: tion 1Predicting Secondary Structure Which of the following peptides is more likely to take up an…
A: Amino acids Proteins are the polymers of nitrogenous compounds called amino acids. Each amino acid…
Q: QUESTION 4 Which of the following amino acids is not positively charged at pH 7? O Lysine O Arginine…
A: An amino group and an acid group are present in organic molecules called amino acids. Amino…
Q: QUESTION 13 Which amino acid below would represent a favorable gain in enthalpy when interacting…
A: Enthalpy ( H) is the measure of heat evolved or consumed during biochemical interactions.…
Q: QUESTION 4 Which of the following amino acids or types of amino acids is rarely found in beta…
A: Beta sheets are the structures made up to anti parallel beta strands. Huge aromatic aminoacids like…
Q: QUESTION 37 Which of the following amino acid residues form hydrogen bonds with Ala residues located…
A: The alpha-helix is a rigid, rod like structure that forms due to the helical conformation of the…
Q: QUESTION 1 What TYPE of inhibition is observed in the following plot: V KK [S], mM m Competitive…
A: Enzyme inhibition decreases the catalytic activity of the enzyme. Inhibition of the enzyme may be…
Q: Question 5 The core protein of a proteoglycan is noncovalently attached to: O oligosaccharides.…
A: The proteoglycan is major component of extracellular matrix in animals. Together with proteoglycans,…
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- Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSNQUESTION NO.1which of the following are chemical characteristics of monosaccharides? A. They contain multiple hydroxyl groupsB. they contain an aldehyde or ketone group C. They contain a branching carbon backbone D. They contain a carbon-carbon double bond E. Every carbon in a monosaccharide is fully reduced F. Every carbon in a monosaccharide is a chiral centerQUESTION NO.2 glucose absorption is hindered by _________ deficiency A. Retinol B. Thiamine C. Potassium D. Sodium E. Ascorbic acid F. Calciferol QUESTION NO.3 phospholipids is made primarily from A. L-glycerol 1-phosphate B. L-glycerol 3-phosphate C. D-glycerol 3-phosphate D. -glycerol 1-phosphate E. sn-glycerol 1-phosphate F. sn-glycerol 3-phosphateQuestion:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
- QUESTION 16 Peptidyl transferase activity (peptide bond enzyme activity) is associated with what site in the ribosome? E P A XQUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibitionQuestion:- 2) oxaloacetate (OAA) occurs as an important intermediate in 2 metabolic processes a) indicate these reaction steps where OAA occurs b) indicate structure for OAA 3) how many reduced equivalents (as electron carrier) are obtained after an oxidation of C16H12O2? describe in detail the structure of these steps.
- Question No.1 (1) A positive Tollen’s test classifies a monosaccharide as a reducing sugar. (2) The bond which links the two monosaccharides of a disaccharide together is a peptide bond. (3) Monosaccharides cannot be broken done into simpler units by hydrolysis reactions. Which of the following statements are true? Question No. 2 : Assuming that a strand of DNA has the following sequence: 5'-AACCGGTT-3' What is the sequence of complementary strand of DNA, from the 5' to the 3' direction?QUESTION 6 What is the three ketter code for each peptide(a) KFYV(b) ERSC(c) PIMFThe 3-letter code for Peptide (a) is: The 3-letter code for Peptide (b) is: The 3-letter code for Peptide (c) is:Question 22: which of the following secondary structures would you expect to find on the surface of a globular protein? Alpha helix Beta sheet Loops between two alpha-helices None of the above because water would disrupt the hydrogen bonding that stabilizes these structures A,B and C as long as the polar and charged amino acid side chains face the surface of the protein.
- QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…QUESTION 5 [20]Describe and compare the metabolism of carbohydrates, lipids and proteins and in your answer, explain the role of ATP. Also discuss the differences between anabolic and catabolic pathways, the regulation of metabolic pathways and the differences in metabolism between the well-fed and 1.1 Describe the structural characteristics that are common to all the amino acids that are found in mammalian proteins and draw the structure of the tripeptide Tyr-Thr-Trp in the ionic form that predominates at pH 7. Show all atoms (including hydrogens) as well as any charges as necessary. Explain the general features of amino acid side chains and the importance of associated non-covalent interactions. (1fasting state.QUESTION NO. 1L-Carnitine is synthesized primarily in the liver but also in the kidneys and then transported to other tissues. It is most concentrated in tissues that use fatty acids as their primary fuel, such as skeletal and cardiac muscle. In this regard, L-carnitine plays an important role in energy production by conjugating to fatty acids for transport from the cytosol into the mitochondria. L-carnitine shuttle is an example of A. ion driven active transport B. facilitated diffusion C. simple diffusion D. ATP driven active transportE. symport F. antiportQUESTION NO.2 Statements: (1) Glucose is both a hexose and a aldose. (2) There can never be more than three enantiomers for a molecule. (3) All common disaccharides have beta-one-four linkages. Which statements are true?
