7) Canavan disease is a gene-linked neurological disorder, in which the brain degenerates into spongy tissues riddled with microscopic fluid-filled spaces. Canavan disease has been classified as a group of genetic disorders termed leukodystrophies. In the normal population, oligodendrocytes carry out an essential developmental task by producing myelin sheets, which constitute the fatty coverings that act as insulators around nerve fibers in the brain and provide nutritional support for nerve cells. In patients with Canavan disease, many oligodendrocytes do not mature and instead die, leaving nerve cell projections known as axons vulnerable and unable to properly function.

According to a group of investigators, Canavan disease is caused by a mutation in the gene that encodes for an enzyme called aspartoacylase, which breaks down the amino acid N-acetyl-aspartate. However, a competing laboratory published an article claiming that aspartoacylase mutation is not relevant for the pathogenesis and progression of Canavan disease.

Design an experimental plan to determine who is right. Include all the controls for full credit. Animal models cannot be used

2 In which property of protein, amino acid sides chains?

a) size

b) peptide bonding

c) function

d) donding

2 Wich of this statements its true about protein structure ?

a)Tertiary structure increases protein function, and quaternary structure decreases protein function.

b)Tertiary structure involves three basic forms of protein folding, and quaternary structure involves 4 basic forms of protein folding.

c) Tertiary structure involves all types of bonds (covalent, ionic, hydrogen, and hydrophobic interactions), and quaternary structure involves just hydrogen bonds.

d) Tertiary structure involves the folding of a single polypeptide, and quaternary structure involves the interaction of multiple polypeptides.

3) What process occur when a Ca+ ionbind to protein and this change the protein's dimensional shape?

A) enzyme activation

B) allosteric modulation

C) signal transduction

D) covalent modulation

4 Which molecule release more free energy when its oxidized?

a) fatty acid

b) polypeptide

c)benzonic acid

d)starch molecule

Discuss in extensive detail the Brønsted-Lowry model of acids and bases including equations for the - a. The definition of Brønsted-Lowry acids and bases b. Application of this model to non-aqueous solvents and gas phase reactions c. Relation between acid-strength and solvents d. Factors that influence the strengths of acids and bases

2) The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below. [S](mu*M) 5 10 20 50 100 200 500 vo (mu*Mmin-1) 21 62 92 126 185 210 217 a) Estimate Vmax and Km from a direct graph of vo vs [S] (Michaelis-Menton plot). b) Use a Lineweaver-Burk plot to analyze the same data. What are the values of Vmax and Km? c) If the total enzyme concentration is 100 pM, what is kcat? d) Calculate kcat/Km for this enzyme. Is the enzyme an efficient enzyme?

Coronado industries is planning to sell 1100 boxes of ceramic tile, with production estimated at 670 boxes during May. each box of tile requires 44 pounds of clay mix and a 0.5 hour of direct labor. clay mix costs 0.4 per pound and employees of the company are paid 14 per hour. manufacturing overhead is applied at a rate of 110% of direct labor costs. Coronado has 4400 pounds of clay mix in beginning inventory and wants to have 5000 pounds in ending inventory. what is the total amount to be budgeted in pounds for direct materials to be purchased for the month?

49000

30080

29480

28880

2) A sugar named sugarose induces synthesis of two enzymes from the sug operon of E. coli. Mutations that affect the appearance of these enzymes were mapped to four adjacent loci (A, B, C, and D) in the order A B C D on the E. coli chromosome. Deletion mutants were characterized in haploids and partial diploids, and the results are shown below. (Here, I = enzyme induced normally, i.e., synthesized only in the presence of the inducer; C = enzyme synthesized constitutively; 0 = enzyme cannot be detected.) Deduce which of the following represents enzyme 1, enzyme 2, a promoter, and a repressor.

                                                     Enzyme 1                       Enzyme 2

A^- B⁺ C⁺ D⁺                                                                      I                                   0

A⁺ B^- C⁺ D⁺                                              0                                  I

A⁺ B⁺ C^- D⁺                                             0                                  0

A⁺ B⁺ C⁺ D^-                                              C                                  C

A⁺ B^- C⁺ D⁺ / A^- B⁺ C⁺ D⁺                                   I                                   I

A⁺ B^- C^- D⁺ / A^- B⁺ C⁺ D⁺                           I                                   0

A^- B⁺ C^- D⁺ / A⁺ B^- C⁺ D⁺                                         0                                  I

A^- B⁺ C⁺ D⁺/ A⁺ B^- C⁺ D^-                            I                                   I

After establishing the protein expression laboratory for your company, you have been asked to produce human insulin protein in bacteria. Although you do not have to worry about purification (that is another lab), you do have to express the protein at sufficiently high levels. Note that the gene has already been placed behind a bacterial promoter to allow for bacterial transcription. Answer the following questions regarding this expression:

a) What component or components of the insulin gene will need to be changed in order to get proper expression in bacteria? Why?

b) What would happen if the 5’ cap of the RNA could not be added? Why?  

c) What would happen if GTPase (an enzyme that converts GTP to GDP) activity was blocked? Why?

Using the data in the table, calculate the rate constant of this reaction.

A+B⟶C+DA+B⟶C+D

?=k=

Units