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
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- 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 wordsWhich 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.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 valueWhich 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 bilayerAt 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.
- Why should the BRCA1 protein be considered one of the best macromolecules within proteins? Is BRCA1 the best functionally, structurally, or based on other properties? Please explain in detail. You can give examples with scientific articles related to protein.Which of the following statements about protein folding is incorrect? Select all. GroEL/GroES allow unfolded proteins the chance to fold within an isolated cavity. Heat shock proteins bind to regions of unfolded polypeptides that are rich in hydrophobic residues, preventing inappropriate aggregation. Many molecular chaperones require ATP for proper function. Molecular chaperones are required for the folding of all cellular proteins.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.