A student is given the task of determining the rate of an enzymatic reaction under defined conditions (i.e known substrate and enzyme concentrations; optimal temperature, pH, etc). Assume the student knows nothing about enzymes or how to perform this task. Since you just completed this task virtually, provide a detailed description of the directions you would give the student on how to determine the rate of the reaction? Give sufficient details so that the student with no knowledge of how to complete this task could be successful.

Congenital Galactosemia typically appears only in infants because with maturation, most children develop another enzyme capable of metabolizing galactose. Its incidence is about 1 per 18,000 births. If the infant does not receive treatment then there is a 75% chance of death. Thus, in the United States infants are screened for galactosemia. Galactosemia can be confused with lactose intolerance but galactosemia is a considerably more serious condition because consumption of galactose can cause permanent damage to their bodies. What dietary changes should be made?

Consider the following reaction: S↔P where the rate constant for the forward reaction is k₁, and the rate constant for the reverse reaction is k₂, and Keq= [P]/[S]

Which of the following would be affected by an enzyme? Please answer yes or no and give a short explanation (5-20 words maximally)

a) decreased K_eq

b) increased k₁

c) increased Keq

d) increased Δ G^#

e) decreased Δ G^#

f) increased k₂

g) more negative Δ G⁰

4. The enzyme alcohol dehydrogenase catalyzes the oxidation of ethyl alcohol by NAD+ to give acetaldehyde plus NADH and a proton:

CH3CH2OH + NAD+                  CH3CHO + NADH + H+

The rate of this reaction can be measured by following the change in pH. The reaction is run in 1 mL 10 mM TRIS buffer at pH 8.6. If the pH of the reaction solution falls to 8.4 after ten minutes, what is the rate of alcohol oxidation, expressed as nanomoles of ethanol oxidized per mL per sec of reaction mixture?

The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone. This enzyme is highly specific for the β anomer of glucose and does not affect the α anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose –that is, for solutions consisting of a mixture of β-D-glucose and α-D-glucose. What makes it possible for this test to measure total blood glucose?

• The α anomer of glucose easily converts to the β anomer.
• Both α-D-glucose and B-D-glucose have a free anomeric carbon
• Glucose interconverts between the glucopyranose and glucofuranose forms.
• The β anomer is present in a much higher concentration than the α anomer. 

• Fehling's reagent can only detect the linear form of glucose.
• Fehling's test cannot be used in the lab to estimate the relative amount of glucose.
• Fehling's reagent is not specific to glucose, detecting other reducing sugars.
• Fehling's test cannot detect the presence of the β anomer.

The map of the lac operon is:    POZY  

The promoter (P) region is the start site of transcription through the binding of RNA polymerase before actual mRNA production. Mutationally altered promoters (P^-) cannot bind RNA polymerase. Certain predictions can be made about the effect of P^- mutations. Use your predictions and your knowledge of the lactose system to complete the following table. Insert a “+” where an enzyme is produced and a “-“ where no enzyme is produced. The first one has been done as an example.

Given the Normal DNA Sequence: 5’ –ATG ATC AGA CTA GCT CAC TCG GGA GTG TGA… 3’

Determine what type of mutation occurred in the following mutant DNA.

Mutant I: 5’ –ATG ATC AGA CTA GCT CAC TCG TGA GTG TGA… 3’

a. At what codon number did mutation occurred?

b. Identify the type of substitution point mutation happened

c. What is the resulting amino acid of the codon that was mutated?

d. What is the consequence of that mutation?

17. During transcription, RNA polymerase adds new nucleotides

1. at the carboxy-terminal of the elongating chain
2. at the amino-terminal of the elongating chain
3. at the 3` end of the elongating chain
4. at the 5` end of the elongating chain
5. at both 5` and 3` ends of the elongating chain

17. Different cells of an organism can produce different types of proteins because

1. They have different genes in different cells
2. Same genes are present in all cells
3. Differential expression of genes in different cells
4. Same genes are expressed in all types of cells
5. None of the above

The average kinetic energy of the molecules in a gas sample depends only on the temperature, T. But given the same kinetic energies, a lighter molecule will move faster than a heavier molecule. Where R=8.314 J/(mol·K) and ℳ is molar mass in kilograms per mole. Note that a joule is the same as a kg·m2/s2.

What is the rms speed of O2 molecules at 429 K?

What is the rms speed of He atoms at 429 K?

Glycine is an amino acid with the formula C2H5NO2. Determine the number of moles of carbon in 24.99 g of glycine?

Apamine is a small monomeric peptide toxin present in the venom of the honeybee. It has the sequence: CNCKAPETALCARRCQQH

A It is known that apamine does NOT react with iodoacetate. How many disulfide bonds are present?

B Suppose trypsin cleavage gave two peptides. Where is (are) the S-S bond(s)? (Hints: If cut by trypsin, but still held together by a disulfide bond, count it as a single peptide. Also, do not count a single amino acid as a “peptide.”)

PLEASE ANSWER B!!!! YOU CAN SKIP A IF YOU WANT I CAN FIGURE IT OUT