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.
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- Which of the following statements concerning complete protein hydrolysis is incorrect? Primary structures are preserved Tertiary and secondary structures are disrupted All peptide bonds are broken Water is a reactant in the processWhich of the following are important factors in the folding of globular proteins in the cytosol? Select as many as apply. Non-polar side chains are normally found on the exterior of proteins Proteins are hydrophobic polymers The cytosol is an aqueous environment. Non-polar side chains tend to group together away from water Proteins are composed of nucleotides Proteins contain both polar and non-polar side chains Peptide bonds are very weak and easily brokenWhich of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.
- Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structureWhich 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 are NOT a level of biological structure? macromolecular level cellular/ organelle levels tissue/ organ level organismal level all of the above none of the above Which of the following are steps in the biosynthesis of proteins can be regulated? macromolecular level cellular/ organelle levels tissue/ organ level organismal level all of the above none of the above.
- During the folding of a protein in a buffered aqueous solution, what happens to the entropy of the protein and the entropy of the water? The entropy of the protein decreases while the entropy of the water increases. Both the entropy of the protein and the entropy of the water increase. Both the entropy of the protein and the entropy of the water decrease. The entropy of the protein decreases while the entropy of the water remains constant.which of the following is correct about protein hydration? a- hydrophobic pathces are hydrated first followed by exposed polar side chains. b- the monolayer water that hydreates proteins are those that hydrate ionic, polar, and nonpolar amino acids on the surface of the protein c- polar amino acids are the first hydrated followed by ionic aminio acids d- hydration of hydrophoic patches in proteins is not possibleAt what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acids
- Affinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the aboveKeratin is a type of __________ found in the ______ of humans. On a cellular level, keratin is found in the cytosol, which means its hydrophobic amino acids are ________. Select one: a. amino acid, skin, exposed on the surface of the protein b. protein, hair, exposed on the surface of the protein c. protein, liver, exposed on the surface of the protein d. protein, liver, not exposed on the surface of the protein e. protein, hair, not exposed on the surface of the protein Clear my choiceWhich of the following is not a function of a protein? help fight diseases build tissues such as bone and muscle control the rate of reactions and regulate cell processes store and transmit genetic information