Two co-op students at your start-up company have been asked to evaluate the rate of reaction occurring in atransparent gel particle containing immobilized mouse melanoma cells. The equation for the reaction rateris is:VmaxT'AsKm+CAswhere 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 yourcalculator 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?

An enzyme is a cellular catalyst that speeds up chemical reactions. Proteins that bind to…

Answered: Two co-op students at your start-up…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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After calculating the extinction coefficient for lysozyme above, you convert it into ml mg cm1 units. (You need not do the calculation, just suppose you did). To calculate the protein concentration in your column fractions (W1-3, E1-2), would your calculated extinction coefficient be a better choice than 1.5 mL mg 1 cm1 value listed in the theory section of your pre-lab? Why or why not? (Choose the best response) Yes, because we expect all of the column fractions to be mainly lysozyme. No, because most, if not all, the column fractions are mixtures of 2 or more proteins. Trick question, we should use the values calculated by EXPASY for lysozyme. Yes, because my calculated value is more accurate than values from the literature. ONo, because lysozyme is still stuck to the column and shouldnot be in any of our column fractions.
A sample of a protein is analyzed by CE using a neutral-coated capillary with a total length of 25.0 cm and a distance to the detector of 22.0 cm. Using an applied voltage of 20.0 kV, the protein was detected at a migration time of 16.2 min. The diffusion coefficient for the protein is 2.4 x 10-7 cm?/s. (a) Calculate the apparent electrophoretic mobility of the protein. (b) Calculate the expected number of theoretical plates for the analysis.
= A different Fab fragment binds to lysozyme with a dissociation constant of Ka 10-6 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to this Fab? [F] = ab M
Based on your Lineweaver-Burk plot, what is the mode of PaESBL-1 inhibition by NSAMB? What is the equation for the double-reciprocal plot at 20 nMnM NAMB?
During SDS-PAGE, glycoproteins migrate as relatively diffuse bands, whereas nonglycosylated proteins typically migrate as narrow, well-defined bands. Explain the reason for this difference in electrophoretic behavior.
r^2=6Dt , where D is the diffusion coefficient of thediffusing object and t is the time that the object is allowed to diffuse. If the diffusion coefficient, D, of a small protein is 5 x 10^-10 m2 s-1, how long (on average) does ittake for the protein to diffuse across a parasitic wasp that is 189 um long ?
Suppose that you are tasked to determine the protein concentration of an unknown protein solution via Bradford assay. You prepared six solutions of bovine serum albumin (BSA) with different concentrations. The initial concentration of the BSA stock solution is 7.50 mg/mL. Approximately 200 µL of Bradford Reagent was added to each of these solutions and the absorbance at 595 nm was taken after 5 minutes. See the table below for data on the standard solutions. Standard # A595 BSA conc (mg/mL) 0.000 0.158 2 1.125 0.291 2.250 0.372 4 3.375 0.503 5 4.500 6 5.625 0.675 Determine the protein concentration, in mg/mL, of the unknown solution if its absorbance at 595 nm was 0.248. Note: Final answer format must be x.xx (two decimal places). Round off only in the final answer. Do not round off in the middle of calculation.
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
You will have to dilute your inital Lysozyme stock in order to pipet volumes larger than 10 uL for the Bradford assay. Calculate a dilution of the 10 mg/mL Lysozyme standard needed to create ensure an appropriate final protein range for the Bradford assay - what concentration will your Lysozyme standard be at for the Bradford assay?
An extract of rat liver was prepared by homogenizing 65 g of tissue in 55 mL of buffer (Fraction 1). This extract was assayed for Enzyme X activity. The total activity of Enzyme X in Fraction 1 was 5,650 units and its specific activity was 11.5 units/mg. Fraction1 was then passed down an ion-exchange column and the bound proteins were eluted using increasing concentrations of NaCl. The fractions from the column were assayed for activity of Enzyme X. The fractions containing activity were pooled to give a total volume of 6.5 mL (Fraction 2) The total activity of Enzyme X in Fraction 2 was 4,162 units and the specific activity was 75.5 units/mg. a) What is the % Yield of the ion exchange step? b) What is the Fold purification of the ion exchange step?
SDS-PAGE and Agarose gel electrophoresis can both be used to separate proteins or protein- complexes based on their size. Separation of a multi-subunit protein complex by SDS-PAGE resulted in two bands with molecular weights of 86 KDa and 136 KDa, while separation of the same complex using Agarose gel electrophoresis resulted in two bands with molecular weights of 222 KDa and 444 KDa. Based on this information, which of the following statements is most likely to be correct? O The complex has a molecular weight of 222 KDa O The complex exists as a dimer of homo-dimers O The complex exists as a dimer of hetero-dimers SE O The complex exists as a trimer, but the individual protein subunits are covalently crosslinked to each other
Protein analysis by gel electrophoresis a). Using the gel image provided to calculate the electrophoretic relative mobility as a ratio of the distance of protein migration to the distance of the tracking dye migration (See Appendix B). If your dye front is not visible, measure the mobility relative to the bottom edge of the resolving gel. Include a labeled print-out of your gel image with your report. b). Plot log MW of the protein markers and commercial myoglobin vs. mobility. Determine the molecular weight of myoglobin obtained after the final purification step (Sample E) from the equation of the line. Submit a copy of your graph along with the gel image. c). Compare your sample E and commercial myoglobin with the ladder. Summary your results. order of sample (left to right) is : A B C D blank E blank Commercial Myoglobin Molecular Ladder

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