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The monod model relates bacterial growth to substrate utilization.   (i) The relationship of growth-limiting substrate utilization to bacterial growth is what is at the heart of the model.   (ii) The mathematical equations of the model can vary in complexity depending on the given conditions   (iii) Endogenous decay is the only mechanisms of cell death that is important enough to warrant representation in the monod model.   Group of answer choices   1.Only (i) and (ii)   2.Only (i) and (iii) are correct   3.(i), (ii) and (iii) are all correct

Two co-op students at your start-up company have been asked to evaluate the rate of reaction occurring in a transparent gel particle containing immobilized mouse melanoma cells. The equation for the reaction rate ris is: Vmax T'As Km+CAs where R=3.2 mm, Vmax= 0.12 gmol s' m3, CAS = 41 gmol m3, and Km=0.8 gmol m3. One student reports a reaction rate of 1.6x10 gmol st; the other reports 1.6x10 1º gmol s1. You left your calculator on the bus this morning, but must know quickly which student is correct. Use an order-of- magnitude calculation to identify the right answer. Which student is correct?

Sketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.

Consider a negatively charged protein adsorbed on anion-exchange gel at pH 8. (a) How will a gradient from pH 8 to some lower pH be useful for eluting the protein? (b) How would a gradient of increasing NaCl concentration (at constant pH) be useful for eluting the protein?

To approximate the concentration of enzymes in a bacterial cell, assume that the cell contains equal concentrations of 1,000 different enzymes in solution in the cytosol and that each protein has a molecular weight of 100,000. Assume also that the bacterial cell is a cylinder (diameter 1.0 μm, height 2.0 μm), that the cytosol (specific gravity 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this hypothetical cell.

The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?

Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?

Please answer fast 1) Amino acid sequence of a heptapeptide gave thefollowing information Asp, leu, lys, ,met, phe and Tyra) Trypsin had no effectb) PITC analysis gave the phenyl alanine derivativec) Chymotrypsin (which cleaves after aromatic amino acids) gave a dipeptide and atetrapeptide, which contained Leu, Lys and Metd) Cyanogen bromide, which cleaves after methionine residues, gave a dipeptide,tetrapeptide and free lys What is the sequence?

From this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions.   Parameters required for calculation of coefficient (Kd) for unknown protein   Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo

Follow up question:... The answer given in problem 31. 17 is inadequate for me, and I simply don't understand the explanation for the answer...  The problem is: Ribosoms were isolated from bacteria grown in a "heavy" medium (13C and 15N) and from bacteria grown in "light" medium (12C and 14N). These 70S ribosoms were added to an in vitro system engaged in protein synthesis. An aliquot removal serveral hours later was analyzed by density-gradient centrifugation. How many bands of 70S ribosoms would you expect to see in the density gradient? Is it possible to give a more comprehensive explanation?  :)  Expert Solution Step 1 Introduction :- A ribosome is a sophisticated molecular machine that produces proteins from amino acids during the process of protein synthesis, also known as translation. Protein synthesis is a fundamental operation that all live cells must carry out. Step 2 Answer :- One light band, one heavy band, a hybrid of light 30S and heavy 50S, and a hybrid…

Below is a picture of a molecule called StemRegenin-1 (SR-1) interacting with a polypeptide at positions A, B, and C. For position A, 1) describe the intramolecular force responsible for binding SR-1, and 2) suggest an amino acid that would provide the force you chose in part 1. B Blank # 1 Blank # 2

Velithin a ceu to the exterior 6s' the ceu 4) A cell from a human heart is placed in a solution containing 90% water. The cell itself has a solute concentration of 30%. a) Sketch the shape of the cell before and after it is placed in the solution for a prolonged period of time. ( /2TI) AFTER BEFORE b) What type of environment was the cell placed in? ( 1TI) c) Which word can describe what took place in this cell? ( /1TI)

Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine   A) I, II, III B) I, II C) I D) II E) I, III

Question:- Part A) How does the molecular mechanism of elongation arrest by SRP differ between Bacillus and Mammalian systems? Please list all the differences and why. Thank you and please explain. Part B) List four interactions of the Ffh M domain in SRP mechanism.

3) What specific proteins might be targeted for up- or downregulated adsorption when designing an implantable material? Please list at least two for each.

We considered the effects of many parameters in designing bioreactors. Please answer the following questions regarding bubbles in airlift fermenters. Bulleted lists are okay. (a) Why was it undesirable to use a very large bubble size (Diameter >7 mm)?  (b) Why was it undesirable to use a very small bubble size (Diameter <7 mm)?  (c) Other than varying bubble size, what can be done to further decrease cell death due to entrainment?

2)Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. Which protein would move toward the positive electrode? choose all that applies. Cytochrome C Myoglobin Hemoglobin Serum Albumin

Under certain conditions, E. coli cells grow from a concentration of 0.1 to 0.5 kg/m 3 in 1 hour. a) Assuming that growth is exponential in this period, what is the specific growth rate of these cells (per hour)? For the above data (growth of E. coli cells), how many hours would it take to grow cells from 0.1 to 1.0 kg/m3? Assume exponential growth during this period.

Electrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu  - Hb Y: Asp replaced by Leu  - Hb Z: Glu replaced by Lys  What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.

For the following proteins in the figure answer the questions below:   A) Oligomerization state of the protein and molecular weight of each protomer B) Number of domains of one protomer and its potential function. C) Based on the information obtained, how many bands will you observe if you run a solution of the spike oligomer in an SDS-PAGE get and in a native gel?

While working with eukaryotic cell cultures, certain requirements such as apparatuses, reagents, ethical approvals etc. are necessary. What are the requirements of a laboratory dedicated to animal cell culture experiments? As a cost effective replacement, what other types of organisms are being experimented upon for preparation of complex proteins?

2.58. Bacteria have equivalent diameters of 2 × 10-6 m and densities of approximately 1 kg/L. Under optimal conditions, bacteria can di- vide every 30 min. Determine the mass of bacteria that would accumulate in 72 hr under continuing optimal growth conditions. Can this occur? Explain.

The physician ordered platinum 100 mg/m2 iv to infuse over 6 hours once 4 weeks for a patient who has a bsa of 1.66m2. (a) how many mg of this antineoplastic drug should the patient receive? (b) if the dose of cisplatin were administered in 1,000 ml d5 1/2 ns, at how many ml/hr would the iv run?

If the number of cells in a bacterial culture rises by a factor of two in one generation, and n is the duration as determined by the formula in equation 1, N is the number of people in the group (2") No way ——- (1) (a) Calculate the number of cell divisions in 4 hours assuming the bacterial cell divides every 20 minutes under normal settings; (b) Calculate the number of cells generated after 4 hours assuming the bacterial cell divides every 20 minutes under standard conditions. (c) Under the same circumstances, how long will it take to make 8192 cells? (d) Calculate the hours if one bacterium cell divides every 30 minutes.

(a) The octapeptide AVGWRVKS was digested with the enzyme trypsin . Which method would be most appropriate for separating the products: ion-exchange or gelfiltration chromatography? Explain. (b) Suppose that the peptide was digested with chymotrypsin . What would be the optimal separation technique? Explain.

200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.