List 2 proteins that facilitate protein folding and briefly describe the role each play in the lifetime of a protein
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List 2 proteins that facilitate protein folding and briefly describe the role each play in the lifetime of a protein
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- Discuss the role of molecular chaperones in protein folding, and list some important examples of chaperonesDifferentiate the stepwise stages in protein folding.Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?
- Describe the machanism of protein folding, highlighting the roles of chaperons.Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm valueDescribe how proteins interact with membranes and how membrane-spanning motifs within proteins may be identified
- . Theoretical and experimental measurements show that in many cases, the contributions of ionic and hydrogen-bonding interactions to AH for protein folding are close to zero. Provide an explanation for this result.,What are the FOUR ways that protein function is regulated (function turned ON/OFF). Explain each.The elegance and importance of proper protein folding and assembly cannot be overstated. Simple electrostatic interactions are fully responsible for long peptide chains becoming giant, globular, functional proteins. Research and discuss two examples of improper protein folding. What is the cause of each malformed protein? What is the consequence of this deformity? What are potential treatment options, and how do they address and remedy the problem?
- A particular DNA sequence encodes for MRNA that then encodes for the amino acid glutamate in a protein. A mutation occurs in the DNA that changes the MRNA codon for the glutamate into a different codon. Which change would cause the least disruption to the structure of the protein? Hint: Think about the nature of the various R groups (side-chains) of the amino acids, and how intermolecular forces/interactions govern the way a protein folds into its three-dimensional structure. The codon for the glutamate is changed into a stop codon. The codon for the glutamate is changed into the codon for aspartate. O The codon for the glutamate is changed into the codon for phenylalanine. O The codon for the glutamate is changed into the codon for serine.Proper folding of proteins is essential for their biological activity. In general, the functional conformation of a protein is the conformation with lowest energy. This means that if an unfolded protein is allowed to reach equilibrium, it should assemble automatically into its native, functioningfolded state. Why then is there a need for molecular chaperones and chaperonins in cells? What different roles do molecular chaperones and chaperonins play in the folding of proteins?Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..
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