Can you answer all the parts to this question please A. Where does a low barrier hydrogen bond (LBH) form transiently during the serine protease mechanism? B. What part does this LBH play in the serine protease mechanism?
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Can you answer all the parts to this question please
A. Where does a low barrier hydrogen bond (LBH) form transiently during the serine protease mechanism?
B. What part does this LBH play in the serine protease mechanism?
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- A child with coarse facies, corneal clouding, joint stiffness and mental retardation is found to have a Damage to this enzyme directly affects which of partial defect in N-acetylglucosaminotransferase. the following biochemical functions? A. Formation of polysomes B. Microtubule attachment to centrioles C. Synthesis of ribosomal RNA D. Targeting of enzymes for lysosomes E. Transport of sugars into mitochondria10. Answer ALL parts of this question. Prostaglandin-endoperoxide synthase 2, also known as cyclooxygenase- 2 or COX-2, is an enzyme that in humans is encoded by the PTGS2 gene. (a) Explain how this enzyme facilitates prostaglandin biosynthesis by highlighting two key functions. (b) Describe one role for the COX-1 enzyme. (c) Name one condition that the selective COX-2 inhibitors Vioxx (Rofecoxib) and Celebrex (Celecoxib) were used to treat. (d) Name and draw the chemical structures of 4 other small molecule OCOX-2 inhibitors and identify 3 similarities/common features with respect to Rofecoxib and Celecoxib. (e) Name a therapeutic reason for targeting COX-3. Describe the function and therapeutic utility of non-steroidal anti- (f) inflammatory drugs.Which disease occurs when homogentisic acid oxidase is defective?
- Describe the mechanism of action of 1 cycle of the ubiquitin (Ub) ligase system. Describe how the E1, E2 and E3 ligases work to covalently link Ub to the target protein, including which uses an energy source (and how), and the operative amino acids on the enzymes, Ub and target proteinBovine insulin is composed of two polypeptide chains that are linked together covalently. The two chains have the following sequences: GIVEQCCASVCSLYQLENYCN - A chain FVNQHLCGSHLVEALYLVCGERGFFYTPKA - B chain a. Through which amino acids are these two chains linked together covalently? b. How many different ways can these two chains be linked? c. Of the different connectivities you enumerated in part b, which is the biologically active form?When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
- Protein hydrolysis is an exergonic process,yet the 26S proteasome is dependent on ATP hydrolysis for activity. (a) Explain why ATP hydrolysis is required by the 26S proteasome. (b) Small peptides can be hydrolyzed without the expenditure of ATP. How does this information concur with your answer to part a ?Diisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195. Which statement is true of DIPF's inhibitory mechanism? DIPF randomly modifies all serine residues on the protein, and if enough is added, the serine in the active site will eventually be modified. DIPF approaches serine 195 more closely than other substrates. DIPF looks like the substrate for chymotrypsin and binds in the active site as a competitive inhibitor. Serine 195 is in an environment that gives it a higher than normal reactivity with respect to DIPF.Proteinase K should be used as the first step of DNA purification (before applying phenol CIA mixture) to remove most proteins. Proteinase K alone cannot remove all proteins from the lysate. Explain why the Proteinase K enzyme cannot remove ALL proteins from the cell lysate.
- Match the enzymatic activity with the proper description within the ubiquitin-proteasome pathway. Drag and drop options on the right-hand side and submit. For keyboard navigation... SHOW MORE ✓ E1 E2 E3 Proteasome = ||| = ||| = ||| Degradation Ubiquitin-activating enzymes Ubiquitin-conjugating enzymes. Ubiquitin ligasesThe steps of the chymotrypsin mechanisms are listed below (1-7). Put the steps of chymotrypsin mechanism in the correct order. Figure representing chymotrypsin mechanism is given for reference. a.The portion (N-terminal end) of original substrate with the new C terminus diffuses away b. Substrate binding c. His 57 catalyzes removal of H from Ser 195 hydroxyl; Ser 195’s nucleophilic O attacks carbonyl C of substrate; tetrahedral intermediate is formed d. Water binding; water is deprotonated by His 57; resulting OH nucleophilically attacks carbonyl of remaining substrate; tetrahedral intermediate is formed e. His 57 donates H to N of…prpc is a normal protein of our neuronal cell membrane that is sensitive to protease action (ie can be broken down by protease) true or false?