front 1 List the four major classes of macromolecules. | back 1 Carbohydrates, Lipids, Proteins, Nucleic Acids |
front 2 Distinguish between monomers and polymers | back 2 Monomers are the small molecules that make up a Polymer. A Polymer is a long chain consisting of monomers that are connected by covalent bonds. |
front 3 Condensation and Hydrolysis reactions | back 3 Condensation reaction -> A reaction in which two molecules become
covalently bonded to each other though the loss of a small molecule,
usually water; also called dehydration reaction. |
front 4 Distinguish among monosaccharides, disaccharides, and polysaccharides. | back 4 monosaccharides: simplest carb and is the monomer for disaccharides
and polysaccharides |
front 5 Describe the formation of glycosidic linkage | back 5 A covalent bond formed between two sugars |
front 6 Distinguish between glycosidic linkages found in starch and cellulose. Explain why the difference is biologically important. | back 6 Starch has alpha glycosidic linkages and cellulose has beta glycosidic linkage. Is important because we have an enzyme that breaks down the alpha but not the beta. |
front 7 Describe the role of symbiosis in cellulose digestion. | back 7 Symbiosis: ecological relationship between different organisms (cow,
bacteria), stuff living inside of other things, beneficial and not so
beneficial. |
front 8 Describe the building-block molecules, structure, and biological importance of fats, phospholipids, and steroids. | back 8 Fats: are constructed of a glycerol + 3 fatty acids. (saturated fats
= bad) |
front 9 Identify an ester linkage and describe how it is formed. | back 9 Found in fats and connect a glycerol and three fatty acids. |
front 10 Distinguish between saturated and unsaturated fats. | back 10 Saturated: no double bonds, straight chains of hydrogen and carbon,
solid at room temp |
front 11 Name the principle energy storage molecules of plants and animals | back 11 Plants: starch stores the energy |
front 12 Distinguish between a protein and a polypeptide | back 12 Protein: many structures, wide variety of functions, made up of
polypeptides |
front 13 Explain how a peptide bond forms between two amino acids. | back 13 A dehydration reaction covalently bonds amino group of one amino acid with carboxyl group of another amino acid |
front 14 List and describe the four major components of an amino acid. Explain how amino acids may be grouped according to the physical and chemical properties of the R group. | back 14 Amino group |
front 15 Explain what determines protein conformation and why it is important. | back 15 Polypeptide has to have best environment(temp,pH). Important because if not in good conditions it unravels and can not do the right job. (denaturation) |
front 16 Explain how the primary structure of a protein is determined. | back 16 primary structure: DNA tells the amino acid order. bonded with peptide bonds. |
front 17 Name two types of secondary protein structures. Explain the role of hydrogen bonds in maintaining secondary structure. | back 17 Secondary: Alpha Helix and Beta Pleated Sheet |
front 18 *Explain how weak interactions and disulfide bridges contribute to tertiary protein structure. | back 18 tertiary structure has disulfide bridges. covalent bond. ionic bonding. hydrogen bonds. vanderwalls. needs all of these bonds to keep the right shape. |
front 19 List four conditions under which proteins may be denatured. | back 19 heat, acid, salt |
front 20 List the major components of a nucleotide and describe how these monomers are linked to form a nucleic acid. | back 20 nitrogen base, pentose sugar, phosphate group |
front 21 Distinguish: | back 21 pyrimidine: C.T.U. (think structure of DNA) |
front 22 Briefly describe the three-dimensional structure of DNA | back 22 A double-helix consisting of two anti-parrallel nucleotide strands. There is a spiral around an imaginary axis |
front 23 Be able to explain why chaperonins are sometimes necessary and how they may assist in proper folding of proteins. | back 23 The folding is not always spontaneous. They keep amino acids from inappropriate associations. |
front 24 List and briefly describe three complementary approach to determining a portion structure | back 24 Primary Structure: the unique amino acid sequence that determines a
protein's structure and function. Any slight changes, deletions,
insertions or substitutions in the amino acid sequence can have a
great impact on the protein's ability to function |
front 25 Explain how DNA or protein comparisons may allow us to assess evolutionary relationships between species | back 25 shared traits and features account for us being descended from one another |