Assume you know or have access to the sequence of DNA or a protein unless the question states that its sequence is unknown.

You are investigating an anti-cholesterol drug designed to lower LDL but not HDL. The drug interferes with lipid processing by blocking a conversion enzyme. Some reports from the clinical trials indicate that people with a SNP in the conversion enzyme gene sequence do not respond to the drug. Explain how could you develop an experimental model to determine if the mutation is involved in a lower response to the drug?

How does the Near Attack Conformation (NAC) contribute to enzyme function? How can an enzyme put a substrate into an energetically unfavorable conformation? How does modern drug design utilize NAC? Please go into detail, provide examples, and use diagrams to help illustrate your explanation. Especially use diagrams please.  

NAC means "Near Attack Conformation". I am struggling to understand how all of these relate. Thank you so much for the help!

~ALL OF THESE PARTS ARE STRICTLY ASKING ABOUT The Antibiotic Degrading Enzyme, NOT ANTIBIOTIC RESISTANCE IN GENERAL~ the more specific the better; preferably typed, as to be legible; thank you so much in advance

Please describe to me the mechanism of and behind the form of antibiotic resistance of antibiotic degrading enzymes (like what the processes that it works under). Also, which class of antibiotics does the mechanism of antibiotic degrading enzymes attack? Finally, which antibiotic-resistant bacteria are using the mechanism employed by an antibiotic degrading enzyme.

1. (3%) You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data are obtained: [S] V0 –Inhibitor +Inhibitor 0.0001 33 17 0.0002 50 29 0.0005 71 50 0.001 83 67 0.002 91 80 0.005 96 91 0.01 98 95 0.02 99 98 0.05 100 99 0.1 100 100 0.2 100 100

a) What is the Vmax in the absence of inhibitor?

b) What is the Km in the absence of inhibitor?

c) When [S] = 0.0004, what will V0 be in the absence of inhibitor?

d) When [S] = 0.0004, what will V0 be in the presence of inhibitor?

e) What kind of inhibitor is it likely to be?

2. (2%) An enzyme is inhibited by two distinct competitive inhibitors, IA and IB. IA is shown to bind with a Ki of 13 μM while IB binds with a Ki of 150 μM.

a) Which is the more potent of the two inhibitors?

b) The natural substrate for the enzyme has a Km value of 0.1 mM. How does the substrate binding affinity compare to each of the two competitive inhibitors?

3. (2%) Assuming they have equal affinity for the enzyme, why would a noncompetitive inhibitor be a more effective drug than a competitive inhibitor?

Materials:

Reaction Buffer 0.5 M Tris HCl pH 8.0 with 5 mM MgCl2

Alkaline phosphatase: 500 μg/mL stock solution in the buffer above. Keep enzyme on ice!

p-nitrophenyl phosphate: 1000 μM and 10000 μM stock solutions in reaction buffer

1) Using the enzyme stock solution above and the dilution equation, calculate the volumes needed to prepare 2 mL of three enzyme dilutions consisting of 100 μg/mL, 125 μg/mL, and 150 μg/mL. Use the reaction buffer to make these dilutions.

2) Calculate the amount of substrate needed for each of the following concentrations 10 μM, 25 μM, 50 μM, 100 μM, 200 μM, 500 μM, 1000 μM, and 2000 μM using the two stock solution concentrations listed above. Use the 1000 μM stock solution to calculate dilutions from 10-200 μM and the 10,000 μM stock solution to calculate from 500 μM-2000 μM. The final volume is 1.0 mL (or 1000 μL) for each dilution. Also calculate the volume of buffer needed, given that we will add 100 μL of the enzyme solution and the final volume is 1.0 mL (or 1000 μL) for each dilution.

1) Match the following with their definitions

___ Kinase

___ Methylation

___ DNA ligase

___ Topoisomerases

___ Single- Stranded Binding

___ Exonuclease

A) Protiens that bind to and protect the unpaired DNA strands during replication.

B) Enzyme that relives the supercoiling strain due to the twisting of the DNA strands ahead of the replication fork.

C) Enzyme that removes an incorrect nucleotide from a growing DNA strand

D) Enzyme that phosphorylates other molecules

E) Enzyme that acts as "glue" upon removal of Okazaki fragments or DNA repair, binding the DNA strands back together

F) The method by which we can identify the older, parental DNA strand.

2) Match the following cellular processes with the phases of meiosis. You can only have one answer per question, but answers may be used more than once.

___ The meiotic spindle disappears

___ Synapsis occurs

___ Microtubules from both poles of the spindle move bivalents to the

center of the cell

___ Microtubules attatch to kinetochores at the centromeres on bivalents

___ The nuclear envelope re-forms around the segregated chromosomes

that contain sister chromatids

A.) Prophase I

B) Prophase II

C) Prometaphase I

D) Prometaphase II

E) Metaphase I

F) Metaphase II

G) Telophase I

H) Telophase II

I) Anaphase I

J) Anaphase II

Glycine residues occur in a higher percentage in proteins than any other amino acid.  Suggest two reasons why.

Membrane lipids in tissue samples obtained from different parts of the leg of a reindeer show different fatty acid compositions. Which of the following statements is/are true?

Multiple answers: You can select more than one option

A

Because reindeer spend much time walking through ice and snow the proportion of unsaturated fatty acyl chains should increase from the top of the leg (warm) to the hoof (cold) to insure fluidity at low temperature.

B

Unsaturated fatty acids closer to the hoof have a lower melting point due to the presence of double bonds.

C

The presence of double bonds prevent unsaturated fatty acids from packing together tightly.

D

The presence of saturated fatty acids help membranes to remain fluid at low temperature.

E

Saturated fatty acid content should be higher at the top of the leg (warm compared to the hoof) exhibiting a higher melting point due to the absence of double bonds.

​(Analyzing the quality of firm​ earnings)  ​Kabutell, Inc. had net income of $800,000​, cash flow from financing activities of $70,000​, depreciation expenses of $60,000​, and cash flow from operating activities of $600,000.

a.  Calculate the quality of earnings ratio. What does this ratio tell​ you?

b.  ​Kabutell, Inc. reported the following in its annual reports for 2011-2013

Calculate the average capital acquisitions ratio over the​ three-year period. How would you interpret these​ results?

Illustrate and explain how an elevation in plasma glucose levels leads to glucose-stimulated insulin secretion by pancreatic β-cells. Your illustration and explanation should include GLUT2, Glycolysis, TCA Cycle, Oxidative Phosphorylation, ATP, ATP:ADP, Kir6.2, calcium channel, synaptotagmin, secretory granules, proinsulin, insulin, and C-peptide.