H3. Draw the Lineweaver-Burk plots for the reaction that your selected enzyme is involved with and without the inhibitor. PROTEASE / RİTONAVIR
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H3. Draw the Lineweaver-Burk plots for the reaction that your selected enzyme is involved with and without the inhibitor. PROTEASE / RİTONAVIR
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- Can you help me, please? Enzyme inhibition (compare and contrast reversible and irreversible inhibitors)Hello, I am comparing the four types of enzyme inhibition. Kidnly please fill out the table for me :)Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.
- The ability of an enzymes active sites to bind only substrates of compatible shape and charge is known as ________. selectivity specificity subjectivity specialtyPlease answer clearly and directly Explain what is meant by Optimum pH. Does pH lower than optimum pH denature the enzyme? How about pH higher than optimum value?Parallel lines on a Lineweaver-Burk plot are diagnostic of— noncompetitive inhibition. allosteric activation. competitive inhibition. allosteric inhibition. uncompetitive inhibition.
- The oxyanion hole of a serine protease has which of the following roles (select all correct answers)? Question 3 options: Acid-base catalysis Proximity and orientation effects Transition state stabilization Induced fitMultiple choice correct answer and explain every point 2. The factors that contribute to the enhancement of the rate of reactionsa) Specific inhibitor macromoleculesb) Product inhibitionc) Availability of substrate and activator cofactord) Covalent catalysise) Proximity and orientation effectsYou have performed protein purification on your new favorite enzyme using a protocol which involves the following steps/samples: crude extract, ammonium sulfate cut, ion exchange and gel filtration. You need to run 25ug of protein from your crude extract sample on an SDS-PAGE gel. You have determined that the protein concentration of your crude extract sample is 2.1mg/ml. Your total sample volume is 30ul. You have water for your diluent and 6x SDS-loading dye to prepare your sample. List the components of your prepared sample. Note: you will only have access to a P20 and a P200 to prepare this sample.
- Help me, I don’t understand. For the one substrate and for all 4 substrates. I will really appreciate itEnzyme inhibition (compare and contrast reversible and irreversible inhibitors)From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of trypsin. The amino acids and residues should be represented by the three-letter abbreviation.