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 productivefolding.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.

Molecular chaperones interact with unfolded or partially folded protein subunits, and help them in…

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. V Each protein has its own "assigned" chaperone to assist in its proper folding. O Misfolded proteins are innocuous and readily cleared by the cell. O The native structure of a protein is entirely encoded in its amino acid sequence. V Misfolded proteins often aggregate in large structures in the cell. O Misfolded proteins are thermodynamically stable versions of a protein.

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. V Each protein has its own "assigned" chaperone to assist in its proper folding. O Misfolded proteins are innocuous and readily cleared by the cell. O The native structure of a protein is entirely encoded in its amino acid sequence. V Misfolded proteins often aggregate in large structures in the cell. O Misfolded proteins are thermodynamically stable versions of a protein.

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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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..
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?
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
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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.
. 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.,
The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in a solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface. By determining these exchange rates, we can explore protein-folding reactions, probe the tertiary structure of proteins, and identify the regions of protein-protein interfaces. We can investigate these exchange reactions by studying the behavior of the protein in solvent that has been labeled with deuterium, 2H, a stable isotope of hydrogen. Select the methods that could be readily applied to the study of hydrogen-deuterium exchange rates in proteins. enzyme-linked immunosorbent assay (ELISA) nuclear magnetic resonance (NMR) spectroscopy x-ray crystallography mass spectrometry (MS)
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