2. The common naturally occurring form of cysteine has a chirality center that is named (R), however;

(a) What is the relationship between (R)-cysteine and (S)-alanine?
(b) Do they have the opposite three-dimensional configuration (as the names might suggest) or the same configuration?
(c) Is (R)-cysteine a D-amino acid or an L-amino acid?

Consider a 0.487 L solution of the amino aspartic acid (0.685 M), which ahs a carboxylic acid group (pKa = 2.10), an amine group (pKa = 9.82), and a carboxylic acid side chain (pKa = 3.86). How many liters of 2.59 M NaOH would you need to add to reach the isoelectric point of the amino acid?

Based on what you know about transcription, RNA processing, and translation, how can a single sequence variant have different effects on the amino acid sequence across the transcript variants of a gene? How can a single sequence variant appear in different amino acid positions in the polypeptides translated from transcript variants of a single gene?

A 55.0 mL solution of 0.126 M potassium alaninate (H2NC2H5CO2K) is titrated with 0.126 M HCl. The pKa values for the amino acid alanine are 2.344 (pKa1) and 9.868 (pKa2), which correspond to the carboxylic acid and amino groups, respectively. a) how do you calculate the PH of the first equivalent and b) the second equivalent? please help

Which best explains why fatty acids produce more energy per carbon than glucose?

a. Glucose must proceed through more pathways to yield ATP

b. Fatty acids are already located in the mitochondrial matrix

c. Glucose molecules are already partially oxidized

d. All of the above

Choose the correct type of expression for each example.

An enzyme acts as a catalyst in the fermentation of A to form product R. An aqueous feed stream containing the enzyme and compound A flows into a CSTR at 25 L/min, and the initial concentration of A is 2 mol*L^-1 . Determine the volume of the CSTR (in Liters, expressed to the nearest integer ) needed to achieve 98% conversion of reactant A. You may assume that the enzyme concentration and volumetric flowrates are constant. The maximum rate of destruction of the substrate is 0.4 mol/(L min). When the substrate concentration is 0.5 mol/L, the rate of destruction of the substrate is 0.2 mol/(L min), i.e. half of the maximum rate.

You are provided with the following portion of a protocol:

Determine concentration of enzyme stock solution, if unknown, by taking an A_{280 nm} reading of a 1:100 dilution (in water). Use a total volume of 1 ml in the cuvette.

Dilute some of the enzyme stock with buffer A to make a 4 mg/ml solution.

Serially dilute the 4 mg/ml solution with buffer A to make working solutions of 400 µg/ml and 40 µg/ml.

Prepare 30 µl of each working solution for every sample

The PI of the lab gives you a tube of enzyme and tells you the following before disappearing into the office to write more grant proposals:

There is 50 µl of enzyme stock solution. The enzyme is expensive to purify, so follow the protocol exactly, using as little of the stock solution as possible.

The concentration of the stock solution is currently not known, but a 1 mg/ml concentration of the pure enzyme has an A_{280 nm} of 2.0.

You’ll be performing the assay on 12 samples.

Make enough of each working solution so that you have at least 400 ul to work with when you do the assay (to cover any waste and/or inefficiencies in pipetting).

3. (6 pts) Figure out your plan for making each solution required in the protocol. Be certain you FINISH with the required volumes of EACH solution! a. Calculate what is needed to make the 4 mg/ml solution b. Calculate what is needed to make the 400 ug/ml working solution c. Calculate what is needed to make the 40 ug/ml working solution

QUESTION

Match the following molecular biology techniques to their correct descriptions.

5 points   

QUESTION 2

Which of the following DNA sequences could potentially be a recognition site for a restriction enzyme?

YES = The sequence could potentially be a recognition site for a restriction enzyme.

NO = The sequence could NOT potentially be a recognition site for a restriction enzyme.

(a) 5' TGCGCA 3'   YES NO

(b) 5' TGCTGC 3'      YES NO

(c) 5' ATTTTA 3'   YES NO

(d) 5' GGATCC 3'   YESNO

(e) 5' CGCG 3'   YESNO

(f) 5' AGGAGG 3'   YES NO

HINT: You will need to generate the complementary strand.

1) Evaluate the double integral ∬Dx^2 y dA, where D is the top half of the disc with center the origin and radius 2 by changing to polar coordinates.

2) Use a double integral to find the area of one loop of the rose r= 6cos (3θ).

3) Use polar coordinates to find the volume of the solid below the paraboloid z=50−2x^2−2y^2 and above the xy-plane.