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

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

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

See similar textbooks

Similar questions

Is it possible to draw the figure with all the figure visas by hand? Note : The drawing should look like a student drawing and not an expert drawing, please make the marking on the drawing complete and in a clear line away from mixing words
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
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
Which one of these is correct ? And why are the rest incorrect?
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…
There is a "primary driving force" behind protein folding (to form tertiary structure). This driving force can be used to explain below phenomenon except: water has a high density and a high boiling temperature non-polar amino acids go inside a protein long chain fatty acids form micelles oil spills go to the surface of water phospholipids form lipid bilayer
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.
A membrane-spanning protein segment has to adopt a regular secondary structure, because— Secondary structures facilitate the aggregation of nonpolar groups to increase stability. The hydrogen–bonding requirements of the polypeptide backbone have to be satisfied. α helix and β sheet have dimensions perfectly fit into the space created by the lipids. The regular structural features make it easy to align with lipid molecules in the membrane. Secondary structures can be packed tightly to minimize the surface areas.
The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.