On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a cysteine protease. Cysteine proteases
Q: A diploid organism with a 45,000-kb haploid genome contains 21% G residues. Calculate the number of…
A: According to Chargaff's rules, DNA from each cell of any organism should contain a 1:1 ratio (base…
Q: a. What is the classification of the Arabinose in terms of combined no. of carbons and highest…
A: The five-carbon sugar arabinose is extensively distributed in nature and can be the only carbon…
Q: Amino acids with ionizable side chains are found in all groups except: negatively-charged…
A: There are four classes of biological macromolecules: proteins, nucleic acids, lipids,…
Q: A hypothetical protein has a molar mass of 23,300 Da. Assume that the average molar mass of an amino…
A: Amino acids are organic compounds that combine to form proteins; thus, they are known as protein…
Q: The isoelectric point of eIF4a is 5.02. Students are given a sample of cell lysate containing eIF4A…
A: Ion Exchange Chromatography (IEC) is a chromatography technique whose ability to separate analytes…
Q: The diagram shows the catalytic hydrolysis of sucrose into the molecules glucose and fructose by the…
A: There are four classes of biological macromolecules: proteins, nucleic acids, lipids and…
Q: Part B Calculate the nonequilibrium concentration of ethanol in yeast cells, if AG = -38.3 kJ/mol…
A: The free energy of a reaction is represented by ∆G. Under standard conditions, it is represented as…
Q: most amount of attraction to an anion column operating at the physiological ph
A: pH (Potential of Hydrogen):It is a measure of the acidity or alkalinity of a solution.It quantifies…
Q: After exhalation of carbon dioxide, His 146 becomes in O Protonated; Increased O Deprotonated;…
A: The statement is describing the Bohr effect, which is a phenomenon where the binding of oxygen to…
Q: ration Determine how reaction rate (velocity) varies with substrate concentration. Rate increases…
A: Q.Explanation:- Substrate is a specific term for the reactant on which a particular type of enzyme…
Q: TPCK is a molecule with large hydrophobic groups. Why does TPCK inactivate chymotrypsin but not…
A: Proteases are enzymes responsible for cleaving peptide bonds. Chymotrypsin and trypsin are both…
Q: Penicillinase, also known as ß-lactamase, is a bacterial enzyme that hydrolyzes and inactivates the…
A: The Michaelis-Menten equation is a mathematical equation that relates the rates of enzyme-catalyzed…
Q: Which mutation will most likely cause the mutant or protein to misfold in terms of thermodynamics.…
A: Mutations are the permanent change in DNA sequence. These changes may occur naturally or by inducing…
Q: How can molecular structural analysis be accomplished with electrospray ionization mass…
A: Molecular structural analysis involves determining the arrangement and properties of atoms within a…
Q: The value of AGO for the conversion of 3-phosphoglycerate to 2-phosphoglycerate (2PG) is +4.40…
A:
Q: You will now build a 15 amino acid peptide using another paper or wire backbone as you did above.…
A: Peptides are polymers of amino acids. Proteins are primarily peptides. There are 20 general…
Q: =) D) CH₂ H₂N CH₂ CH₂ NH3 H3NCH-Coo CH₂ OH -CH-COO CH-OH CH3 H3NCH-COo CH-CH3 C10 NH₂
A: There are 20 naturally occurring amino acids in nature. Out of these 10 are essential and 10 are non…
Q: Show the location and the molecule that provides electrons to the electron transport chain and trace…
A: The electron transport chain (ETC) plays a vital role in cellular respiration, occurring within the…
Q: Choose a FALSE statement about Hill's plot. All or none binding is given by n = N² (N is the total…
A: Hills plot is a graphical representation used in biochemistry to analyze the cooperative binding of…
Q: The following plot (percent of O2 bound versus [02]) shows three possible curves (A, B, C). In this…
A: The association between the partial pressure of oxygen (PO2) and the percentage of hemoglobin…
Q: Which of the following would not increase efficiency of transfer of oxygen from hemoglobin to…
A: Haemoglobin is a transport protein that helps in carrying of respiratory gases like oxygen and…
Q: Predict the products of this organic reaction: CHI O CHÍCH CCHCHI CHO 4 NaOH Ang Specifically, in…
A: When you mix a compound that has an ester in it with sodium hydroxide (NaOH), something interesting…
Q: complete the sentence. In the Sanger method, the carbon atom of the reagent fluorodinitrobenzene…
A: The Sanger reagent (1-fluoro-2,4-dinitrobenzene) is used to determine the N-terminal amino acid in…
Q: Write the name of a naturally-occuring nonpolar amino acid. (You will find the structures of the…
A: The proteins are composed of twenty naturally occurring amino acids that are connected via peptide…
Q: The change in Gibbs free energy under biochemical standard-state conditions is represented by AG°'.…
A: Details
Q: How do antibiotic-rich environments like hospitals speed up the rate at which superbugs increase…
A: It is the condition when bacteria evolves mechanics to make the antibiotics used against them as…
Q: A membrane simulator is shown below. Watch the video clip in order to answer the question. Diffusion…
A: Osmosis is the movement of water molecules across a semipermeable membrane, driven by the difference…
Q: What is an insulin
A: Hormones are chemicals that specialized glands synthesize and produce in order to control and…
Q: Which of the following molecules is amphipathic? Select all that apply. Select all that apply A…
A: Molecules that have a polar region and non-polar region within the same molecule. The polar region…
Q: HB is a poor transporter of oxygen OHB is an efficient transporter of oxygen HB is an efficient…
A: Hemoglobin is a pigment which is present in red blood cells. It is made up of 4 polypeptide chains…
Q: 2. Assuming no contact inhibition and optimal nutrient and waste transport, graph the cell…
A: a. The cell proliferation rate (kp) is a measure of how quickly cells divide. A high kp value means…
Q: Refer to the figure below, what are the following forces of attraction is involved in the protein…
A: The tertiary structure of the protein is a 3D structure established and stabilised by the…
Q: gel filtration chromotagrpahy
A: Chromatographic techniques:These are a diverse group of laboratory methods that are used for the…
Q: Please provide explanations and work for each part of the question. If able to keep the same format…
A: Protein structure is a fundamental concept within biochemistry, encompassing the hierarchical…
Q: The place on the enzyme where the substrate binds is called the: a) coenzyme b) transition state…
A: An enzyme is usually made up of protein with different amino acids linked together by peptide bonds.…
Q: 3. Aspartate aminotransferase (AspAT) catalyzes the following reaction: COO™ C=O CH₂ COO…
A: Km is sometimes thoughtlessly used as an indicator of affinity of an enzyme for its substrate. But,…
Q: After completing your analysis of the different bacterial methyltransferases at MethylTranspharmiX,…
A: Reversible enzyme inhibition can be of 4 types generally. They…
Q: Using a biochemical technique called site-directed mutagenesis, it is possible to substitute a…
A: Site-directed mutagenesis is a method employed in the lab to perform accurate and deliberate…
Q: 19. Draw all 20 of the genetically encoded amino acids at (a) pH = 1; (b) pH = 1; (c) pH = 12.…
A: Amino acids are organic compounds that form the building blocks of proteins in cells. The structure…
Q: Which of the following is/are true regarding SDS-PAGE (there may be more than one correct answer,…
A: SDS-PAGE is the abbreviation for Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis.It is a…
Q: d) If the [GTP/[GDP] falls to 2.0, calculate G, keeping all other concentrations the same including…
A: The Krebs cycle which is also known as the TCA cycle (tricarboxylic acid cycle) or Citric acid…
Q: A biochemist has 100 mL of a buffered solution at pH 7.5. The concentration of the buffer is 0.1 M,…
A: According to Henderson-Hasselbalch equation, find the ratio of acid and it's base.pH = pKa + log…
Q: I believe ut should be Asn Ala Val Tyr Ala Arg Met Tyr
A: A peptide is a short chain of amino acid residues linked together via a peptide bond. As per the…
Q: Are the given examples representative of acid-base catalysis, covalent catalysis, or metal ion…
A: Enzymes are proteinaceous entities that help the precedence of chemical reactions. The reactions…
Q: What would be the free-energy change generated by the import of one mole of Na+ from a concentration…
A: In order to find the free energy change () associated with import of 1 mole of Na+, first we need to…
Q: Which nucleotide forms are used in the cellular reactions for DNA replication? a. 3' triphophates b.…
A: DNA replication is the process by which a new DNA molecule is synthesized using an already existing…
Q: Biological membranes are selectively permeable, allowing certain molecules to cross the membrane,…
A: The cells or the plasma membrane is the outermost layer enclosing the cell. It is responsible for…
Q: Draw a diagram of the hydrogen bonding interactions in: i) a two-stranded antiparallel beta sheet,…
A: Secondary structure of protein: Formed due to twisting of polypeptide chain.The folding is due to…
Q: Put these three molecules in the order of most oxidized to least oxidized. нн нс-с-н нн H > > 0=…
A: In chemistry, the concept of oxidation state plays a crucial role in assessing the degree of…
Q: +H₂N-CH-COO™ 1 CH₂ I CH₂ I CH₂ I +H₂N-CH₂ A. amino acid D O amino acid B amino acid C O amino acid A…
A: Amino acids are biomolecules that have a hydrogen atom, an amino group and a carboxyl group linked…
Trending now
This is a popular solution!
Step by step
Solved in 3 steps with 1 images
- complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
- In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectivelyIf the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex? Leu Val O Asp O LYS QUESTION 15 What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanine residue? (n) His Asp Nucleophilic affack by water stabilization of a metal ion covalent catalysis electrostatic attraction of the substrate O acid base catalysis 789 Mustly cloudy Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. here to searchIn this step of purine biosynthesis, which functional group gets activated by ATP Pribose NH, ATP Carboxyaminolmidazole ribonedeotide Asp AD Fumarate Pribose NH, S-Aminolmidazole- 4(N-succinylcarboxamide) ribonucleotide O Carboxyaminoimidazole ribonucleotide COOH O Carboxyaminoimidazole ribonucleotide NH2 O Asp side chain COOH O Asp main chain NH2 O Asp main chain COOH
- The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is Adraw the complete mechanism of lysozyme (SN2) beginning with the disaccharide N-acetyl muramic acid - to N acetyl glucosamineThe rate of the peptidyl transferase reaction increases as the pH increasesfrom 6 to 8. Explain these results in terms of its reaction mechanism.
- erioiogy e cell walls of Gram-positive and Gram-negative bacteria are structurally different but both contain peptidoglycan. Which TWO of the following statements about peptidoglycan biosynthesis are CORRECT? O Peptidoglycans are made from alternating units of N-acetylmuramic acid and N-acetylglucosamine. O N-acetylglucosamine is synthesised from N-acetylmuramic acid by the addition of acetic acid derived from phosphoenolpyruvate. O Peptidoglycan synthesis in Gram-positive bacteria involves the addition of the amino acids, L-alanine, D-glutamic acid, L-lysine, to N-acetylmuramic acid. O D-glutamic acid-D-glutamic acid dipeptide is linked to the tripeptide side chain of N-acetylmuramic acid to form N-acetylmuramic acid-pentapeptide O At the beginning of the biosynthesis pathway, the N-acetylglucosamine-N-acetylmuramic acid-pentapeptide-phospholipid crosses the cell membrane and is added to growing peptidoglycan chain. O The transglycosylase enzyme is located on the inner face of the…Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.The glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?