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Body Structures & Functions

Body Structures & Functions

12th Edition

ISBN:9781285695495

Author:Scott

Publisher:Scott

Chapter3: Cells

Section: Chapter Questions

Problem 5C

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pls help ASAP, thank you! “which feature of protein folding is NOT accurate?”

Which feature of protein folding is NOT accurate?
Proteins generally fold to their lowest free energy state.
O Misfolded or unfolded proteins contribute to a variety of disease
states.
Protein folding is largely due to a gain in the protein's
conformational entropy.
The primary sequence largely determines the folded protein
structure.

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Based upon your knowledge of protein folding, which of the following statements would you expect to be FALSE: O The native state is the protein conformation with the most negative Gibbs free energy value. O The hydrophobic effect causes non-polar side chains to pack into the interior of a protein away from solvent. Proteins are likely to try out every possible conformation before folding into the native state. O A protein incubated in hexane (C6H14) is likely to denature and unfold. O Detergents can interact with the side chains of valine, leucine and phenylalanine.
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? A mutation in the genetic sequence, which ultimately causes an amino acid to change(e.g. Trp – Asn – His turns into Trp – Arg – His) Dissolving a protein in a non-polar solvent (like oil) instead of water.
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, functioning folded state. Why then is there a need for molecular chap- erones and chaperonins in cells? What different roles do molecular chaperones and chaperonins play in the folding of proteins?
Which of the following statements about protein folding and structure are true? Check all that apply. Chaperones, like the GroEL-ES complex, work by providing a sequestered environment in which proteins can safely explore the conformational space towards productive folding. O Chaperones "know" how to actively fold proteins into their proper final structure. Each protein has its own "assigned" chaperone to assist in its proper folding. O Misfolded proteins are innocuous and readily cleared by the cell. V The native structure of a protein is entirely encoded in its amino acid sequence. Misfolded proteins often aggregate in large structures in the cell. Misfolded proteins are thermodynamically stable versions of a protein.
Which of the following constitutes the primary structure of a protein? O the folding of a polypeptide chain the polypeptide chains stacked on top of each other O the linear sequence of amino acids in a polypeptide chain several polypeptide subunits
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?
Protein denaturation is the disruption of a protein's secondary to quaternary structures. Protein denaturation is always reversible. [, O The FIRST statement is TRUE. O The SECOND statement is TRUE. O BOTH statements are TRUE. O NONE of the statements are TRUE.
Which of the following levels of protein architecture is least likely affected by changes in pH? O Secondary Structure Quaternary Structure O Tertiary Structure O Primary Structure
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..
Which of the following amino acids are more likely to be on the interior of the protein? And which are more likely to be exposed to the surface? L I D E W A V K H M Q Y
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 value
In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing?

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