Match the following levels of protein structure with their appropriate definition or description: This level of structure occurs when multiple subunits - each an independent polypeptide chain - combine by non-covalent interactions to make a functional protein. Choose... This level of structure is a listing of amino acids in order from amino to carboxyl terminus. Choose... This level of structure is maintained by interactions between atoms found in the side-chains ("R-groups") of amino acids. Choose... This level of structure is composed of either alpha-helices or beta-sheets. Choose... Which of the following statements is TRUE regarding bonds in polypeptides? Select one: a. Double bonds stabilize secondary structures. b. The alpha carbon bonds are all polar. c. The double bond between C=N leads to a trans conformation. d. Peptide bonds allow free rotation of each amino acid relative to the others.
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Match the correct level of protein structure to the statements below. You can use an answer more than once. a) Primary amino acid sequence b) Hydrogen bond c) Antiparallel β-sheet d) Disulfide bond e) Hemoglobin consists of 4 polypeptide chains f) The lysozyme molecule contains regions of helical structure g) Hydrophobic interactions h) Salt-bridges Levels of Protein Structure: Primary Secondary Tertiary Quaternary
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Match each property with the level(s) of protein structure. Choose the best answer in each case. Examples of this are alpha-helices and beta-pleated sheets. Results from repetitive hydrogen bonds between atoms in the peptide backbone. Can be altered when a protein is reversibly denatured. Results from covalent bonds formed between an amino group and a carboxyl group. Results from covalent bonds between two S-containing R-groups. Results from covalent or non-covalent interactions between R-groups within one polypeptide chain. Is also known as the protein sequence. Results from covalent or non-covalent interactions between different polypeptide chains. Results from non-covalent interactions between the R-groups.
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