Concept explainers
To review:
The given blank space in the statement, “maintains the helical structure of many proteins: ______; links polypeptide chains and can cause protein to bend: _____ and _____; joins the two strands of double helix: ______; links amino acids to form the primary structure of protein; _____.
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Biology: Life on Earth Plus Mastering Biology with Pearson eText -- Access Card Package (11th Edition)
- A mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)arrow_forwardThe protein hemoglobin, consisting of four polypeptides (two a-globin chains, with 141 amino acids each, and two b-globin chains, with 146 amino acids each), contains how many peptide bonds? 570 peptide bonds 571 peptide bonds 572 peptide bonds 573 peptide bonds 574 peptide bondsarrow_forwardYou put albumin, the protein responsible for lipid transport through the blood, in methane, a hydrophobic solution. Would you expect albumin to still be functional? Yes the protein would still be functional because its primary structure remains intact Yes the protein would still be functional because it is used to carry lipids No the protein would not be functional because the peptide bonds would be dehydrated No the protein would not be functional because covalent bonds weaken and disrupt secondary structure No the protein would not be functional because the tertiary structure would change to maximize hydrophobic interactionsarrow_forward
- Which of the following does not contribute to the tertiary structure of protein? a. ionic interaction b. H-bond c. peptide bond d. hydrophobic interactionarrow_forwardWhich one of the following types of bond is principally responsible for holding the α-helix shape of a protein secondary structure : A) peptide B) disulfide C) hydrogen D)ionicarrow_forwardWhich of the following statements about proteins is correct? There are 20 types of amino acids commonly found in proteins. Proteins are composed of glyosidic bonds. Proteins are never folded. They do not contain any hydrophilic or hydrophobic residues. Peptide bonds are composed of only carbon and oxygen atoms.arrow_forward
- What type of bonding is present in the primary structure of proteins? A. peptide bond B. hydrogen bond C. ionic bond D. more than one choice is correctarrow_forwardThe following is an example of which level of protein structure? What bonds form this level of structure? Asp-Met-Leu-Trp-Gly-Asn-Lysarrow_forwardWhich of the following IS NOT a type of interaction that helps create a protein’s tertiary structure? Select one: a. glycosidic bonds b. hydrogen bonds c. salt bridges d. disulfide bondsarrow_forward
- Which of the following statements regarding hydrogen bonding in secondary structures is true? Both α-helices and β-sheets only use intrachain hydrogen bonds. Both α-helices and β-sheets only use interchain hydrogen bonds. α-helices only use intrachain hydrogen bonds and β-sheets can use either intrachain or interchain hydrogen bonds. α-helices can use either intrachain or interchain hydrogen bonds and β-sheets only use interchain hydrogen bonds.arrow_forwardWhich of the following is true about the structure of nucleotides? A. Purine nucleotides cannot base pair with pyrimidine nucleotides. B. Pyrimidine bases are larger than purine bases. C. Purine and pyrimidine bases are found in DNA and RNA. D. Thymine base is found in DNA and RNA.arrow_forwardProteins are the dominant structural and functional molecules in a cell. Which one of the following statements about proteins is NOT correct? A. The native conformation of a protein is usually arrived at very quickly after synthesis. B. Hydrogen bonding is the only type of bonding that gives rise to secondary structure. C. Urea denatures proteins by disrupting the interactions among non-polar (hydrophobic) amino acids D. Most proteins consist of a single polypeptide and thus do not have quaternary structure.arrow_forward
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