3 (m) Compare and contrast the variety of amino acids with that of monosaccharides and fatty acids. Which group exhibits the greatest structural variability? 2 (n) How does the molecular structure of urea suit its bio- logical function? 3 (o) Describe the appearance and arrangement of amino acids in \alpha-helix and \beta-pleated sheet regions of polypeptides. What type of intermolecular forces are involved in maintaining protein secondary structure? /3 (p) Describe and give examples of proteins that have a variety of tertiary structures. Relate the tertiary struc- ture of these proteins to their biological functions.
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2 In which property of protein, amino acid side chains? a) size b) peptide bonding c) function d) bonding 2 Which of these statements is true about protein structure? a) Tertiary structure increases protein function, and quaternary structure decreases protein function. b) Tertiary structure involves three basic forms of protein folding, and quaternary structure involves 4 basic forms of protein folding. c) Tertiary structure involves all types of bonds (covalent, ionic, hydrogen, and hydrophobic interactions), and quaternary structure involves just hydrogen bonds. d) Tertiary structure involves the folding of a single polypeptide, and quaternary structure involves the interaction of multiple polypeptides. 3) What process occurs when a Ca+ ion binds to a protein and changes its dimensional shape? A) enzyme activation B) allosteric modulation C) signal transduction D) covalent modulation 4 Which molecule releases more free energy when it is oxidized? a) fatty acid b) polypeptide c) benzoic acid d) starch molecule
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3. Match the description with the key terms given below in blue: --- polymerization macromolecule peptide dehydration hydrolysis a. A protein is a polymer built by linking together amino acids which are monomers. The bond that links amino acids together in a protein is called a peptide bond. b. In a dehydration (also called condensation) reaction, 2 or more molecules combine to form a larger molecule with the loss of water. c. A hydrolysis reaction breaks apart another molecule by adding water. 4. Name the four groups of macromolecules of life and fill in the table (with the following key words): CHO CHONS CHONP CHO with lots H lipid carbohydrate Nucleotides amino acids monosaccharides glycerol & fatty acids nucleic acids Polysaccharide DNA, RNA proteins fats, oils, steroids, phospholipids, wax Group Elements Monomer Polymer Functions 1. carbohydrate Quick energy Energy storage Structure of cell walls 2. 3. 4.
1) Which two functional groups are always present on an amino acid? What is the "R" group of the amino acid? 2) How many different kinds of amino acids are found in typical cells? How are they similar, and how do they differ? 3) What is a peptide bond, and how does it result in the backbone of a polypeptide consisting of a chain of repeated N-C-C-N-C-C-...? Where do the R groups attach to this chain? 4) What is meant by the primary structure of a protein? Why is this considered a central determinant of protein shape, even though it does not have any physical shape features? 5) What are the two basic motifs in the secondary structure of a protein? What do they look like? (In other words, if you had to describe them to a child, what familiar object would you compare them to?) 6) Why is protein shape such an important factor? What is denaturation, and how does it affect the protein's usefulness in the living cell where it was produced? 7) What is an enzyme? What does it do to help the cell succeed? Why are enzymes usually sensitive to changes in temperature, i.e., working well at body temperature but failing at very high temperatures?
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