Write and describe about the important of Protein and Amino Acids Test in healthcare or industry.

Note: The report must not exceed 3 pages minimum (NOT include references), type of test, purposes and the important of the test with reliable references

subject biochemestry

Biochemistry question:

Describe the four levels of proteins structure (primary, secondary, tertiary and quaternary). Make sure to describe the role of non-covalent interactions involving the main chain or side chains of the amino acids that form to stabilize the structure.

What are the key differences between glycolysis in the liver and in muscle? Why is this important for the function of those different types of cells/tissues within the human body?

Glycolysis requires four different phosphotransferase reactions. Identify the phosphoryl donor, acceptor, and nucleotide end-product for each. The choices for each box are the same and they are 1,3-Bisphosphoglycerate, ADP, ATP, Fructose-6-phosphate, Glucose, Phosphoenolpyruvate.

Regulation of GNG and glycolysis

1. Describe how high energy charge favors gluconeogenesis over glycolysis based on the ratio of [ATP]/[AMP] of high energy charge and allosteric regulation (McKee page 298).
2. Describe how low energy charge measured by low ratio of [ATP]/[AMP] inhibits the rate of GNG based on allosteric regulation of fructose 1,6 bisphosphatase by AMP.
3. Compare the rates of GNG and glycolysis in a liver cell with low energy charge based on allosteric regulation.
4. Differentiate between the blood concentrations of insulin and glucagon hormones based on the period after a carbohydrate meal
5. Differentiate between the blood concentrations of insulin and glucagon hormones based on fasting period
6. Differentiate between regulation by hormone and energy charge based on the time frame of the response
7. Differentiate between regulation by hormone and energy charge based on the locations in which hormones and allosteric effectors bind with respect to the cell
8. Describe how hormones regulate enzyme activity by phosphorylation based on a series of reactions that start with hormone binding (see video lecture).
9. Differentiate between stimulation of glycolysis and GNG based on a cell stimulated by insulin
10. Differentiate between stimulation of glycolysis and GNG based on a cell stimulated by glucagon.
11. Describe how increase in oxaloacetic acid (OAA) concentration stimulates glycolysis based on Le Chatelier’s principle.

Consider an ion channel membrane protein:

•Even amino acids with non-polar R groups have unavoidable polar regions—where?

•Given this, why do you suppose most transmembrane domains exist as α-helices or β-sheets (what does this allow?)

•Describe the types and locations of amino acid R groups that would be found at various surfaces of this ion channel. How would this contribute to the pore’s function as an ion channel?

Choose one of these answers for each question: succinyl CoA, glycerol, apolipoprotein, chylomicron, liver, monoacylglycerol and 2 fatty acids, proprionyl CoA, adipose cells, triacylglycerol, acetyl CoA, muscle, hormone-sensitive lipase, bile salts, diacylglycerol and 1 fatty acid, mitochondria, glycerol and 3 fatty acids, and lipase.

1. storage form of lipids  

2. large particle that transports dietary fats through the blood stream

3. secreted by the gall bladder to help emulsify dietary fats in the intestines

4. digested dietary fats cross the plasma membrane into intestinal cells in this form

5. enzyme used to digest dietary fats in the intestines

6. site of significant fat storage in the body

7. enzyme activated by PKA that digests stored triacylglycerols

8. digested stored fats exit the cell in this form

9. this product of digestion of stored triacylglycerols is used by the liver for gluconeogenesis

10. produced from oxidation of even-number chains of fatty acids

A study is made of amino acids in the hemolymph of millipedes. For a sample of four males and four females of each of three species, the following concentrations of the amino acid, alanine (in mg/100 ml), are determined:

Species 1 : (Male) 21.5, 19.6, 20.9, 22.8; (Female) 14.8, 15.6, 13.5, 16.4

Species 2: (Male) 14.5, 17.4, 15.0, 17.8; (Female) 12.1, 11.4, 12.7, 14.5

Species 3: (Male) 16.0, 20.3, 18.5, 19.3; (Female) 14.4, 14.7, 13.8, 12.0

a.) Test the hypothesis that there is no difference in mean hemolymph alanine concentration among the three species

b.) Test the hypothesis that there is no difference between males and females in mean hemolymph alanine concentration.

c.) Test the hypothesis that there is no interaction between sex and species in the mean concentration of alanine in hemolymph.

d.) Prepare a graph of the row, column, and cell means, and interpret it in terms of the results of the above hypothesis tests.

e.) If the null hypothesis of part a, above, is rejected, then perform a Tukey test to assess the mean differences among the species.

1. Which of the following are possible strategies for treating viral infection

1. Blocking uncoating of the virus after entry
2. Blocking synthesis of viral nucleic acids
3. Blocking viral attachment to host cell receptors
4. Blocking insertion of viral DNA into the host cell chromosomes
5. All of the above

2. A double-stranded, enveloped RNA virus that contains reverse transcriptase belongs to which family?

1. Poxviridae
2. Hepadnaviridae
3. Retroviridae
4. Picornaviridae
5. Rhabdoviridae

3. E.coli makes insulin because _.

1. It picked up the insulin gene from another cell
2. It is an ancient gene that now has no function
3. It needs to regulate its cell-glucose level
4. The insulin gene was inserted into E.coli DNA
5. There is no reason. E.coli is unable to make insulin.

4. Which enzyme would cut this strand of DNA : GCATGGATCCCAATGC?

1. Enzyme – EcoRl
2. Enzyme – Hind III
3. Enzyme – Bam HI
4. Enzyme – Hale III
5. Enzyme – Pst I

Carbonic anhydrase catalyzes the reverse reaction (of course!): HCO3 - + H+  CO2 + H2O Initial velocities were measured at the following concentrations of HCO3 - (The enzyme concentration was 0.0025 mg/ml; the enzyme Mr = 29,100 Da.): [HCO3 -] mM 1.3 2.6 6.5 13.0 26.0

vo (µM/sec) 2.5 4.00 6.30 7.60 9.00

vo (µM/sec) with acetazolamide 1.17 2.10 4.00 5.70 7.20

a. Do the required calculations and graph the results as a Lineweaver-Burk plot. Use the X- and Y-axis scales provided or an excel graph; add labels and units to each axis. b. Calculate (i) KM (ii) Vmax and (iii) the enzyme turnover number (kcat).

c) Add a line to the graph corresponding to reactions with the acetzolamide inhibitor. Draw the line with the acetazolamide as either a (i) competitive inhibitor or (ii) noncompetitive inhibitor. What kind of affinity would azetazolamide have for ES or S?