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From the given statement which is false?
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- Which of the following statements about chaperones is FALSE? a. Chaperones prevent incorrect interaction (i.e. aggregation) within and between non-native polypeptides thereby increasing the yield b. Chaperones are proteins c. Chaperones can greatly increase the rate of protein folding, and therefore, chaperones are enzymes. d. Chaperones do not specify correct folding e. Chaperones prevent aggregation of unfolded proteinsWhich 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.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 process
- 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 aboveProtein β-sheets are most likely to be found in: a either the interior or exterior of proteins, with no preference for one or the other. b the exterior of proteins, exposed to the aqueous environment. c the interior of proteins, away from the aqueous environment.when a protein has achieved the _______ level of protein structure, it takes on a 3d shape due to the r group interactions. primary secondary tertiary quaternary
- Protein A will fold into its native state only when protein B is also present in the solution. However, protein B can fold itself into native confirmation without the presence of protein A. Which of the following is true? a. Protein B serves as precursor for protein A b. Protein B serves as molecular chaperone for protein A c. Protein B serves as ligand for protein A d. Protein B serves as structural motif for protein AWhich 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…When a protein is denatured using heat Select one: a. its C-terminal will change. b. its tertiary structure will change. c. its amino acid sequence will change. d. its amino acid composition will change.
- Which way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceedsReductase is the Fe protein composed of two: polypeptide chains linked by three disulfide bonds. polypeptide chains linked by a 4Fe–4S cluster. α subunits and two β subunits. polypeptide chains linked by a 2Fe–2S cluster.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.