Which statement about intrinsically disordered proteins is true?○ They contain small hydrophobic cores○ They represent misfolded conformations of cellular proteins○ Lack of stable three-dimensional structure precludes a role in cellular function○ They are responsible for proteostasis○ They can be central players in protein interaction networks

Out of the given choices, statement 5 is true: Intrinsically disordered proteins (IDPs) can be…

Answered: Which statement about intrinsically…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

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Similar questions

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?
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.
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.
Protein structures have several different levels of organization. In the space below indicate the type of molecular bonds that can contribute to each level of organization: primary- secondary- tertiary- quarternary-
Which of the following regarding disulfide bonds is/are true? Disulfide bonds are the most common intrachain covalent linkage in proteins Disulfide bond formation is critical for correct protein folding into the native conformation Disulfide bonds impart a large degree of stability to the secondary structure of proteins The intracellular environment is too oxidizing to allow disulfide bond formation A and D
Why might adding a strong reducing agent like Dithiothreitol (DTT) help denature an extracellular protein? O Disulfide bonds might be reduced that might be critical in stabilizing its structure O Disulfide bonds might be oxidized that might be critical in stabilizing its structure O Disulfide bonds formed inside the cytoplasm can be oxidized O Cysteines can be reduced to form stabilizing disulfide bonds
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?
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 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
Proteins associate with membranes in a number of different ways. identify them and outline their molecular basis.
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
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

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