A Lineweaver Burke double reciprocal plot is an excellent tool for describing the activity of enzymes...
A Lineweaver Burke double reciprocal plot is an excellent tool for describing the activity of enzymes that have quaternary structure and are allosterically regulated.
A. True
B. False
Homework Answers
Allosteric proteins do not obey michaelis-menten kinetics , hence a Lineweaver burke double reciprocal plot is not an excellent tool for describing the activity of enzymes.
Hence the answer is B,false
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A Lineweaver Burke double reciprocal plot is an excellent tool
for describing the activity of enzymes...
] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is y = 12x...
] a. The equation of Lineweaver-Burk double-reciprocal plot of caffeine dehydrogenase-catalyzed reaction is y = 12x + 3. Calculate Vmax (mmol/s) and Km (mmol/L). b. [5 points] Estimate V for caffeine concentration of 400 mmol/L. c. [10 points] The enzyme caffeine dehydrogenase (Cdh) is an inducible quinone-dependent oxidoreductase. Describe how the addition of caffeine into the culture medium will be detected and transcriptionally regulated by the two-component system in Pseudomonas sp. CBB1.
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is give...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
A plot of 1/V versus 1/[S], called a Lineweaver-Burk or double-reciprocal plot, is a useful tool...
A plot of 1/V versus 1/[S], called a Lineweaver-Burk or double-reciprocal plot, is a useful tool for identifying the type of enzyme inhibition. Modify each graph by dragging the endpoints to show the various types of enzyme inhibition. Competitive inhibition What is the inhibition mechanism for the competitive inhibitor? with inhibitor UNI The inhibitor binds to both free enzyme and enzyme-substrate complexes with identical binding constants. The inhibitor binds only to free enzyme. The inhibitor binds to both free enzyme...
#9 quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
1- Describe two attributes that are different for hemoglobin and myoglobin; focus on characteristics that are...
1- Describe two attributes that are different for hemoglobin and myoglobin; focus on characteristics that are a direct consequence of differences in tertiary and/or quaternary structure. For each attribute, be sure to specifically explain how 3° and 4° organization impacts the described differences. 2- The kinetics of an enzyme (E)-catalyzed reaction are measured over a range of substrate (S) concentrations in the presence or absence of a reversible inhibitor (I). The total enzyme concentration is 10 uM, and the inhibitor...
1. Which of the following statements is FALSE? Helicase activity 'unwinds DNA making the double-stranded molecule...
1. Which of the following statements is FALSE? Helicase activity 'unwinds DNA making the double-stranded molecule into single strands. b. The leading strand of DNA is started by an RNA primer The lagging strand of DNA is synthesized as "Okazaki fragments", cach with its own RNA primer. DNA replication proceeds in both directions around the bacterial chromosome. DNA polymerase synthesives new DNA in one direction (3 to 5) only. 2. Which of the following would be found in eukaryotes? a....
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
thats all the information that he gave us to solve the question. Thank you for trying...
thats all the information that he gave us to solve the question.
Thank you for trying anyways
X C E Question 23 1 pts The free-energy changes for the transfer of individual amino acid residues from a hydrophobic to an aqueous environment are given as follows: Amino acid AG of transfer (kJ/mol Proline -0.8 -12.6 Histidine 6.7 Alanine Methionine 14.3 Based on this information, which of these amino acid pairs is MOST likely to be represented in membrane-spanning alpha helices?...
4. The double-reciprocal transformation of the Michaelis-Menten equation, also called the Lineweaver-Burk plot, is given by: 1 Km 1 1 where, the plot of (1/V.) vs (1/[S]) is a linear plot. If you only know the x-axis and y-axis intercepts from this plot, how can you determine Vmax and Km? (A) multiply the reciprocal of the x-axis intercept by -1. (B) multiply the reciprocal of the y-axis intercept by -1. (C) take the reciprocal of the x-axis intercept. (D) take...
A plot of 1/V versus 1/[S], called a Lineweaver-Burk or double-reciprocal plot, is a useful tool for identifying the type of enzyme inhibition. Modify each graph by dragging the endpoints to show the various types of enzyme inhibition. Competitive inhibition What is the inhibition mechanism for the competitive inhibitor? with inhibitor UNI The inhibitor binds to both free enzyme and enzyme-substrate complexes with identical binding constants. The inhibitor binds only to free enzyme. The inhibitor binds to both free enzyme...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
1. Which of the following statements is FALSE? Helicase activity 'unwinds DNA making the double-stranded molecule into single strands. b. The leading strand of DNA is started by an RNA primer The lagging strand of DNA is synthesized as "Okazaki fragments", cach with its own RNA primer. DNA replication proceeds in both directions around the bacterial chromosome. DNA polymerase synthesives new DNA in one direction (3 to 5) only. 2. Which of the following would be found in eukaryotes? a....
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
thats all the information that he gave us to solve the question.
Thank you for trying anyways
X C E Question 23 1 pts The free-energy changes for the transfer of individual amino acid residues from a hydrophobic to an aqueous environment are given as follows: Amino acid AG of transfer (kJ/mol Proline -0.8 -12.6 Histidine 6.7 Alanine Methionine 14.3 Based on this information, which of these amino acid pairs is MOST likely to be represented in membrane-spanning alpha helices?...
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