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- 5) Using FRAP (Fluorescence Recovery After Photobleaching), you can measure the diffusion rate of membrane proteins. You attach a fluorescent marker to your protein of interest, bleach a small region of the cell membrane with an intense laser light, and determine the time it takes for the bleached spot to recover fluorescent signal (see figure below). (a) (b) Bleach Laser bleaching of fluorescent marker Fluorescence intensity recovery Recovery Time How would the recovery time of your protein change if the membrane contained a higher concentration of unsaturated fatty acids? Why? How would the recovery time of your protein change if you conducted the experiment at a lower temperature? Why? How would the recovery time of your protein change if it were anchored to the membrane skeleton? Why?A drop of a solution containing a mixture of amino acids gly, ala, glu, arg, his was applied to the middle of electrophoretic paper, moistened with a pH 6.0 buffer, and an electric voltage was applied. Indicate in which direction (towards the cathode, anode, or will remain at the start) individual amino acids will move.When run under nondenaturing conditions (without SDS or β-mercaptoethanol), nativepolyacrylamide gel electrophoresis (PAGE) allows proteins to maintain biological activity, so the GFP band should fluoresce when exposed to UV light. How do the staining patterns of gels run in this way differ from the staining patterns of gels run using SDS-PAGE?
- Each of the ff. involves a disorder in the function of an organelle or other cell structure. Identify the cell organelle or cell structure involved and indicate whether it is likely to be underactive or active. a) A baby is placed on a low phenylalanine diet as his newborn screening results revealed that he inherited phenylketonuria. b) A girl suddenly felt weak and manifested cyanide poisoning symptoms after ingesting undercooked cassava which contains cyanoglycosides. c) A man develops pleiomorphic liposarcoma (rare cancer). The cause of the problem is a hard mass of cells in his right inner thigh that rapidly increased in size in a matter of 2 months. d) A male chef learns that he is infertile because his sperm are non-motile. Helping tags: biology, cell biology, cell structure, cell organelleFor 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?B. E- D C A Cell cytoplasm Cell cytoplasm Bacterial Cell A Bacterial Cell B A cross-section of the cell envelope of two bacterial cells, A and B, are shown in the figure. Which label is matched with the correct structure A) O Structure A: peptidoglycan B) O Structure B: teichoic acid C) O Structure C: lipoprotein D) O Structure D: capsule E) O Structure E: S layer Cell exterior Cell exterior
- How many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.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?Scientists are investigating the human DNA (A strand of human DNA is 2.5 nanometers in diameter). a. Consider an ideal scanning electron microscope (neglect all aberrations and electron-sample interactions) operating at 2 kV. i. k What is the electron wavelength? What is the resolution of the microscope? Can this microscope be used for the resolution of the ii. [ iii. ! human DNA? b. What is the main difference between Scanning Electron Microscope and an Optical Microscope? c.[: Can they determine the structure of the the human DNA using optical microscope? Explain your answer.
- 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/mLThis lab examines the relationship between the absorbance of light by a solution at 595 nm and the concentration of the Coomassie Blue dye-BSA protein complex in the solution. State whether the following descriptions of the lab experiment are valid or not, and explain why you say Yes or No: a.The experiment would be significantly more accurate if absorbance readings were recorded for a range of wavelengths, not just for 595 nm.b.The experiment has limited accuracy because it does not account for the absorbance of light by the other components (components that are not the dye-protein complex, such as excess dye that is not bound to any protein) of the solution.c.The absorbance reading measures practically all the protein content in the solutions(50) During an experiment , equal aliquots of Escherichia coil and Staphylococcus aureus are separately sonicated at the same level to mechanically disrupt bacterial cells. E.coli cells are disrupted , but their is minimal disruption of S, aureus cells. Which of the following bacterial structures best explains this difference? (A) Cytoplasmic membrane (B) Outer membrane (C) Peptidoglycan layer (D) Phospholipid bilayer (E0 Polysaccharide capsule