describe a possible mechanism for the dysregulation of molecular chaperones.
Homework Answers
The possible mechanics for dysregulation of molecular chaperons
The molecular chaperons regulate the protein folding to maintain the proper functioning of the protein.
The misfolded or aggregated protein induce cellular toxicity.
This causes a certain degenerative disease called as a polyglutamine disease.
The molecular chaperons help in regulating cell death.
They maintain the protein translocation and degradation of the unfolded protein.
They regulate the signal transduction process and so on. Hence this process is very important to maintain neural and muscular cell activity.
The dysfunction of them causes the cancer cells to produce certain consequences like metastasis, genetic mutation, and hypoxia.
The functioning of the molecular chaperons is shown below:
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describe a possible mechanism for the dysregulation of molecular
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Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein...
Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein folding. One class of chaperone found in organisms from bacteria to mammals is heat shock protein 90 (Hsp90). All Hsp90 chaperones contain a 10 amino acid "signature sequence," which allows for ready identification of these proteins in sequence databases. Two representations of this signature sequence are shown below. (a) In this sequence, which amino acid residues are invariant (conserved across all species)? (b) At...
3. The important function of molecular chaperones to A. move proteins from endoplasmic reticulum to the...
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Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein folding. One class of chaperone found in organisms from bacteria to mammals is heat shock protein 90 (Hsp90). All Hsp90 chaperones contain a 10 amino acid "signature sequence," which allows for ready identification of these proteins in sequence databases. Two representations of this signature sequence are shown below. (a) In this sequence, which amino acid residues are invariant (conserved across all species)? (b) At...
3. The important function of molecular chaperones to A. move proteins from endoplasmic reticulum to the Golgi apparatus B. fold proteins into a native conformation C. add cofactors, coenzymes or prosthetic groups to proteins as they are synthesized D. assemble protein subunits into a quaternary structure E. transport proteins to either the plasma membrane or release them from cells to the extracellular space 4. Protein folding to a native conformation is highly dependent upon all of the following, except: A....
3. There are two possible substitution products fr products and a complete mechanism for their for IUPAC system and circle the major product. Ustitution products from the reaction of 3,3-dimethyl-2-butanol with aq. HBr. Draw the mechanism for their formation, including all intermediates. Name both products based on the :OH MW: 102. Ts-gimo 4. Based on the reaction above, calculate the theoretical yield for the reaction based on 2.0 g of the 3,3-dimethyl-2- butanol and 5 mL of the 48% HBr....
-Trace the general mechanism by which a signal transduction pathway occurs (i.e. from signaling molecule to response) Describe the two ways in which signaling proteins act as molecular switches -Which amino acid residues do kinases typically add phosphate groups? Distinguish between the two types of G proteins -What proteins regulate GTP-binding protein (G proteins) in terms of activation and inactivation? - Distinguish between the three main classes of cell surface receptors.
-Trace the general mechanism by which a signal transduction...
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