Solve part a To begin, you are setting up a melting point measurement assay where you will test membranesmade from four purified components (three fatty acids and cholesterol). Please be sure toclearly label your plots for each of the conditions outlined throughout the problem (ie. you canuse color or dashed and dotted lines to differentiate your curves).•Myristic AcidStearic AcidLinoleic Acid(a) In the space below draw the structures of each of these membrane fatty acids. For the fattyacids also label them with the standard nomenclature we discussed in class. Are any of thefatty acids w-3 or w-6 fatty acids? If yes, indicate which ones.

Fatty acids are the long hydrocarbon chains which can be considered as the building blocks of fats…

Answered: To begin, you are setting up a melting…

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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Proteoglycan aggregates in tissues form hydrated, viscousgels. Can you think of any obvious mechanical reason whytheir capacity to form gels is important to cell function?[Hint: Liquid water is virtually incompressible.]
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?
Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, Ion exchange chromatography is conducted via a software using DEAE-cellulose and method of elution is done by salt gradient. pH is set to 7. In terms of Molar, start of gradient is 0 and end of gradient is 1. The following graph is generated. Using the graph and analytical methods, determine pI of protein.
Our current experimental procedure works because Con A adheres strongly to the nitrocellulose membrane while HRP hardly binds to the membrane at all. If HRP binds as strongly to the membrane as Con A does, our current scheme will not work. Assuming that's the case (HRP strongly binds to the membrane non-specifically, regardless of the presence of ConA), you will need to treat the membrane with an additional solution before treating it with HRP. What solution would that be? O Saturated NaCI solution. O Concentrated HCI. A membrane-binding protein. Concentrated glucose slution.
(A) What property of a protein might make it difficult to transfer it from polyacrylamide gel to nitrocellulose? Explain your reasoning. (B) What parameter of the gel transfer protocol can be adjusted that might help improve the transfer of these problematic proteins to the nitrocellulose membrane? Explain your reasoning. (C) How can we check if proteins have been successfully transferred from the polyacrylamide gel to nitrocellulose?
Of the following cell membrane lipids, which one prefers to reside in the inner leaflet (or inner half) of the membrane bilayer, AND has an overall neutral charge at physiological pH (7.4)? a) PE (phosphatidylethanolamine) is inner-leaflet with an overall neutral charge at pH 7.4 b) SM (sphinogomyelin) is inner-leaflet with an overall neutral charge at pH 7.4 c) PS (phosephatidylserine) is inner-leaflet with an overall neutral charge at pH 7.4 d) PC (phosphatidylcholine) is inner-leaflet with an overall neutral charge at pH 7.4
Given the information and table pls answer the question.Protein XYZ is a heme-containing protein responsible in electron transfer in microalgae. The target protein was extracted using ammonium sulfate fractional precipitation and quantified using Bradford assay. A set of solutions with increasing concentration was prepared using 15.00 mg/mL analogous protein standard [refer to succeeding table]. Each solution was treated with 80 μL of Bradford reagent and diluted to 1.500mL. The absorbance at 595 nm of each solution was obtained and presented below.A 2-mL aliquot of the crude extract was diluted to 10mL with distilled water. The absorbance at 595 nm of this solution was obtained to be 1.1340. Thus, further dilution of the crude extract solution was performed. Two milliliters of the previously diluted solution was treated with 8 mL of distilled water. The absorbance of the final solution at 595 nm was determined to be 0.2150.What is the concentration (in mg/mL) of Protein XYZ in the…
Roughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-
A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
You have purified Protein 'X' and you want to know its concentration. As we learned, you can calculate concentrations by simply measuring UV280 absorbance of protein solutions. Using a UV spectrophotometer, you measured an absorbance of 0.6. Given that Protein X has an absorptivity (or extinction coefficient) of 0.2 mL•mg-cm at 280 nm, what is the concentration of purified protein solution (assume the light path is 1 cm)? -1 O A. 3 g/mL B. 3 mg/mL OC.0.2mg/mL OD.0.2 g/mL OE. 0.6 g/mL
A spherical cell with the diameter of 10uMhas a protein concentration of 20 mg/ml. Determine the number of protein molecules within the cell if the molecular weight of an average protein is 50,000 daltons (g/mol). Recall that Avogadro's number is NA 6.0221367×1023 molecules/mol. =

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