Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 12, Problem 17P
Interpretation Introduction
Interpretation:
The ambiguities of using the hydropathy plots to determine whether the protein is a membrane protein needs to be explained.
Concept introduction:
A graph that is named a hydropathy plot shows the location of an amino acid in a polypeptide and its hydrophobic/hydrophilic nature. This plot can be used to discover clusters of hydrophobic amino acids which show whether the specified polypeptide in the plot is a transmembrane protein or not.
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The above figures show the rate of actin polymerization in the presence of various concentration of profilin (Pfn). In the top figure, flourescence intensity is a measure of total actin that has been polymerized, and this is plotted versus time in seconds. The shade of blue of the lines in the top figure correspond to the shaded blue bars representing various concentrations of profilin in the lower figure. The lower graph shows the initial rates of polymerization of actin plotted again concentration. Which of the following is true:
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- .A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little if any effect from addingarrow_forwardCreate a ROUGH SKETCH (no need for exact hydropathy indices and residue numbers) of the hydropathy plot for the given membrane protein. -coo Please follow the color assignment of the helical domains and properly label the plot and axes. Here is an example: Amino Outside terminus Transmembrane helices are predicted by hydrophobic stretches of 20-25 aa residues 10 50 100 150 200 250 Hydrophobic Inside Hydrophilic Carboxyl terminus -3 10 50 100 150 200 250 Residue number Bacteriorhodopsin Hydropathy indexarrow_forward11:14 structure. They provide the matrix or ground substance of extracellular tissue spaces in which collagen and elastin fibers are embedded. Hyaluronic acid, chondroitin 4-sulfate, heparin, are among the important glycosaminoglycans. 10. Glycoproteins are a group of biochemically important compounds with a variable composition of carbohydrate (1-90%), covalently bound to protein. Several enzymes, hormones, structural proteins and cellular receptors are in fact glycoproteins. Chapter 2: CARBOHYDRATES SELF-ASSESSMENT EXERCISES I. Essay questions 1. Define and classify carbohydrates with suitable examples. Add a note on the functions of carbohydrates. 2. Describe the structure and functions of mucopolysaccharides. 3. Give an account of the structural configuration of monosaccharides, with special reference to glucose. 4. Discuss the structure and functions of 3 biochemically important disaccharides. 5. Define polysaccharides and describe the structure of 3 homopolysaccharides. III. Fill…arrow_forward
- Membrane 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 10arrow_forwardFrom the image. Do you think that a membrane potential exists for this synthetic plasma membrane? If your answer is “yes,” please indicate whether it is negative or positive at the region closer to the inner leaflet of the plasma membrane. Explain your reasoning.arrow_forwardPurification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…arrow_forward
- The hydropathy plot of a particular hyaluronan synthase is plotted by Heldermon et al and is shown below. From this plot, Heldermon et al circled six putative (or predicated) membrane domains (PMDs). Circle the six regions in the plot above you believe could be transmembrane domains of the protein and indicate why you chose those regions. Please include a description of what information a hydropathy plot gives researchers.arrow_forwardPlease help me with this question. More than one answer may be correct. Elastin _______. Options: A) has a repeating structure of 3 amino acids such as Gly-Pro-X B) crosslinks with numerous other elastin peptides to make an elastic fiber C) is physically attached to the smooth endoplasmic reticulum D) is physically attached to ribosomes E) is rich in hydrophobic residuesarrow_forward. The process of a protein folding from an inactive unfolded structure to the active folded structure can be represented by the following equation: unfolded protein = folded protein The values of AH and AS° for the folding of the protein lysozyme are: AH = -280 kJ/mol AS = -790 J/mol · K (a) Calculate the value of AG for the folding of lysozyme at 25 °C. (b) At what temperature would you expect the unfolding of lysozyme to become favorable?arrow_forward
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