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- Cleavage Ligand Precursor Receptor Inactive Receptor Active Cell Membrane 6. The figure above shows a model of a ligand precursor being cleaved to produce an active ligand that binds to a specific receptor. Which of the following is most likely to reduce the binding of the active ligand to its receptor? (A) A change in the cytoskeletal attachment of transmembrane proteins (B) The presence of a large amount of the precursor form of the ligand (C) An increase in the ratio of the number of unsaturated to the number of saturated fatty acid tails of the membrane lipids (D) A mutation in the receptor gene that causes a substitution of a charged amino acid for a nonpolar amino acid in the ligand binding site of the receptorSnipping Tool New L ADAL Q Q- Q At which of the following sites is the characteristic triple helical structure of the collagen initially formed? A. Extracellular space B. Golgi body C. Nucleus T D. Rough endoplasmic reticulum E. Smooth endoplasmic reticulum 부분 C 21 4 3 12 W Beat zoom 3 C Edit in Paint EP CMembrane Protein Insertion in the ER This figure displays five small hypothetical proteins. The a-helix secondary structure of the protein is bracketed and the number of amino acids in the helix is indicated. If the hypothetical ER localization sequence is green-yellow-yellow-green-yellow-red, what protein could potentially be a transmembrane protein in the plasma membrane? = Acidic = Basic = Polar (uncharged) O = Hydrophobic CO₂ T 20 CO2 T 20 NH₂ A. T 20 NH₂ B. NH₂ C. T 20 NH₂ D. NH₂ E. tot 10
- Example Problem: FRAP Data Interpretation The diffusion rate of four different membrane proteins (A, B, C, and D) was measured using a FRAP experiment with purified liposomes. The FRAP recovery curves are shown below. Fluorescence intensity ROI A 3 Time B Time Post-bleaching imaging с Time D Time Pre-bleaching Bleaching imaging imaging (a) Which membrane protein exhibits the higher rate of diffusion in the lipid bilayer? A or B? C or D? (b) Explain the most likely cause of the difference in the recovery curves for proteins A and C.Integral membrane proteins... Choose all that could apply are bound to the membrane by only interacting with the phospholipid's polar head O contain many amino acids with hydrophobic residues O contain alpha-helical membrane spanning domains O would not be digested by trypsin in a permeabilized cell O interact with the phospholipid core of the phospholipid bilayerTONICITY DRAG THE WORDS INTO THE BLANK SPACES BEL@W TO ACCURATELY COMPLETE THE PARAGRAPH Hypertonic Isotonic Hypotonic Hypertonic Lsotonic Hypotonic animal cell plant cell A Above are a represented plant cell and an animal cell. Refer to the key on slide 5 and fill in the blanks below. (If you find yourself counting solute dots, you're working much too hard!) Assume that the cell membranes are allow only water (not the solutes) to pass through. Because the cytoplasms of the plant and the animal cell have equal concentrations of solutes, we can say that their cytoplasms are to each other. If we put both the plant and the animal cells into Solution A, we would expect no change in the cells, because Solution A is to the cytoplasm of each cell.
- HEL 9. Consider the membrane protems in question 7. What cellular functions must always be performed by an integral membrane protein? Explain. NEL 2.2 Membrane Structure and FunctioMultipass transmembrane proteins synthesized by ribosomes on the rough endoplasmic reticulum generally have which of the following arrangements of start-transfer and stop-transfer signals? multiple start signals and multiple stop signals (to allow multiple transmembrane regions) multiple start signals, but only one stop signal (to allow only one transmembrane region) only one start signal, but multiple stop signals (to allow only one transmembrane region) only one start signal, and only one stop signal (to allow only one transmembrane region) only one stop signal, and only one start signal (to allow only one transmembrane region)Or. Foyez Samar The volume enclosed by the plasma membrane of plant cells is often much larger the c corresponding volume in animal cells. The most regsengble explanation for this observation Is that A) plant cells are capable of having a much higher surface-to-volume ratio than animal cells. B) plant cells have a much more highly convoluted (folded) plasma membrane than animal cens. C) plant cells contain a large vacuole that reduces the volume of the cytoplasm. D) animal cells are more spherical, whereas plant cells are elongated. 12 A u
- HC CH reaction with HC CH lysosome CH CH HC CH3 HC CH3 HC CH HC. CH CH3 CH3 ОН OH inside the cell, propranolol sometimes encounters lysosomes, which alter its NH group as shown above (right). reacting with the lysosomes, propranolol becomes trapped inside the cell and can cause psoriasis or other inflammatory side effects. Use IMFS to explain why the altered propranolol gets trapped. Tmolecules of actin could it hold? Assume the cell is spherical The Size of Cells and Their Components (a) If you were to magnify a cell 10,000-fold (typica] of u magnification achieved using an electron microscope), ho ples of Bioch 1. yotic cell with a cellular diameter of 50 µm. (b) If this cell were a muscle cell (myocyte), how many and no other cellular components are present; actin molecules are spherical, with a diameter of 3.6 nm. (The volume of a sphere is %ar.) (c) If this were a liver cell (hepatocyte) of the same dimensions, how many mitochondria could it hold? Assume the cell is spherical; no other cellular components are pre- sent; and the mitochondria are spherical, with a diameter of 1.5 µm. h (d) Glucose is the major energy-yielding nutrient for most cells. Assuming a cellular concentration of 1 mM (that is, 1 millimole/L), calculate how many molecules of glucose would be present in our hypothetical (and spherical) eukaryotic cell. (Avogadro's number, the number of…basic structure of the subunit for each type of cytoskeletal protein and compare and contrast cytoskeletal proteins regarding:– Polarity– General filament structure / relative stability– General intracellular functions