ILLUSTRATIONS. For each of the given proteins: ● Draw the final location of the following proteins after being translocated. ● Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. ● Label the amino and carboxyl ends of the protein. ● Below your drawing, indicate: a. the receptor/s b. the energy source C. if there is signal peptide cleavage or none Endoplasmic Reticulum H₂N- signal seq -COOH retrieval signal sequence
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- II. ILLUSTRATIONS. For each of the given proteins: . Draw the final location of the following proteins after being translocated. • Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. • Label the amino and carboxyl ends of the protein. Below your drawing, indicate: a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none A. Chloroplast H₂N- *SS1 *SS2 -COOH *SS -signal sequenceII. ILLUSTRATIONS For each of the given proteins: ● Draw the final location of the following proteins after being translocated. ● Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: a. the receptor/s b. the energy source C. if there is signal peptide cleavage or none ●. 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?
- Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow.Using the the enzyme acid hydrolase in the lysosome: What is the final destination in which the protein will function? Which features will the protein receive during its manufacture? What is the primary structure (general)? Where is the primary structure made? Where are the secondary and tertiary structures made? Will the protein travel through any organelles during its manufacture? Which ones? What would be the overall result if some part of the manufacture process went wrong, such that the protein ended up as nonfunctional?Classify the fold of each protein. Classify the fold of each domain asall a (or mostly a), all b (or mostly b), a/b, or a+b.. 1. Firmicute collagen-binding protein (1FCB): 2. Bat glycosyltransferase (2BGT): 3. Proteobacterial nitrite sensor (3PNS):
- →x D. Two physical 5. A protein unfolds according to the scheme N properties (property 1 and 2) are measured at three points in the unfolding reaction where the true values of fp are 0.2, 0.5 and 0.8. The corresponding values of K = fx/ fp are 1.0, 0.4 and 0.125. For property 1, d₁ = 0.1; for property 2, d₁ = 0.2. (a) Write an equation that can be used to calculate fapp. (b) Calculate fapp using d₁ = 0.1 (property 1) and fapp using d₁ = 0.2 (property 2). (c) The error in measurement of each physical property is 5 %. Can you detect the presence of the intermediate by measuring the physical properties? Explain your answerPlease help me with this question. More than one answer may be correct. The rough endoplasmic reticulum ______. Options: A) is the only site of protein synthesis in the cell. B) is a site where glycosylation of proteins takes place. C) is a site where cisternal maturation takes place. D) is a location where glutamate carboxylation of proteins take place. E) has a channel through its membrane called Sec61.a. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification b. The chemical properties of an anion exchange column and how it works c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate? d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?
- 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-My PDB code: 3GRS residue point: HIS467 mutation: LEU Describe why this position in your protein is important and outline the effects the mutation will have on the 3D structure and the function of your protein. (up to 50 words)What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a protein with 200 residues after mRNA synthesis, starting from amino acids? Assume that the hydrolysis of PP; is equivalent to the hydrolysis of ATP for this calculation. number of ATP molecules: number of GTP molecules: 400 800 Incorrect