List the four major classes of macromolecules.
Carbohydrates, Lipids, Proteins, Nucleic Acids
Distinguish between monomers and polymers
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.
Condensation and Hydrolysis reactions
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.
Hydrolysis -> A chemical process that lyses, or splits, molecules by the addition of water; an essential process in digestion
Distinguish among monosaccharides, disaccharides, and polysaccharides.
monosaccharides: simplest carb and is the monomer for disaccharides
disaccarides: a double sugar, two monosaccharides bonded together using glycosidic linkage
polysaccharides: a polymer of many monosaccharides
Describe the formation of glycosidic linkage
A covalent bond formed between two sugars
Distinguish between glycosidic linkages found in starch and cellulose. Explain why the difference is biologically important.
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.
Describe the role of symbiosis in cellulose digestion.
Symbiosis: ecological relationship between different organisms (cow,
bacteria), stuff living inside of other things, beneficial and not so
The role in cellulose digestion is bacteria breaks down cellulose for the host cow/bull.
Describe the building-block molecules, structure, and biological importance of fats, phospholipids, and steroids.
Fats: are constructed of a glycerol + 3 fatty acids. (saturated fats
Phospholipids: make up cell membranes; glycerol + 2 fatty acids
Steroid: hormones/cholesterol; four fused rings
Identify an ester linkage and describe how it is formed.
Found in fats and connect a glycerol and three fatty acids.
Distinguish between saturated and unsaturated fats.
Saturated: no double bonds, straight chains of hydrogen and carbon,
solid at room temp
Unsaturated: one or more double bonds formed by removal of hydrogen atoms, liquid at room temperature, bent chains of carbon and hydrogen
Name the principle energy storage molecules of plants and animals
Plants: starch stores the energy
Animales: glycogen(made in your liver) store the energy
Distinguish between a protein and a polypeptide
Protein: many structures, wide variety of functions, made up of
Polypeptide: amino acid sequence (chain), part of the protein
Explain how a peptide bond forms between two amino acids.
A dehydration reaction covalently bonds amino group of one amino acid with carboxyl group of another amino acid
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.
R Group: determines qulaity (polar, nonpolar, etc.)
Explain what determines protein conformation and why it is important.
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)
Explain how the primary structure of a protein is determined.
primary structure: DNA tells the amino acid order. bonded with peptide bonds.
Name two types of secondary protein structures. Explain the role of hydrogen bonds in maintaining secondary structure.
Secondary: Alpha Helix and Beta Pleated Sheet
They are made by hydrogen bonds.
*Explain how weak interactions and disulfide bridges contribute to tertiary protein structure.
tertiary structure has disulfide bridges. covalent bond. ionic bonding. hydrogen bonds. vanderwalls. needs all of these bonds to keep the right shape.
List four conditions under which proteins may be denatured.
heat, acid, salt
List the major components of a nucleotide and describe how these monomers are linked to form a nucleic acid.
nitrogen base, pentose sugar, phosphate group
sugars and phosphates: ladder upright; covalent bonds
bases: rungs of the ladder (purine bonds with a pyrimidine); hydrogen bonds (weakest)
pyrimidine and purine
nucleotide and nucleoside
ribose and deoxyribose
5' end and 3' end
pyrimidine: C.T.U. (think structure of DNA)
example: 5' ATTCGA 3' > 3' TAAGCT 5' : complimentary DNA strands
Briefly describe the three-dimensional structure of DNA
A double-helix consisting of two anti-parrallel nucleotide strands. There is a spiral around an imaginary axis
Be able to explain why chaperonins are sometimes necessary and how they may assist in proper folding of proteins.
The folding is not always spontaneous. They keep amino acids from inappropriate associations.
List and briefly describe three complementary approach to determining a portion structure
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
Secondary Structure: segments of the polypeptide chain that are repeated coiled or folded patterns. This is the result from hydrogen bonding at regular intervals from the hydrogen/nitrogen atoms that are attracted to the oxygen atoms from a nearby peptide bond. Hydrogen bonding either results in alpha helixes or beta pleated sheets.
Tertiary Structure: irregular contortions from interactions between the various R group side chains
Explain how DNA or protein comparisons may allow us to assess evolutionary relationships between species
shared traits and features account for us being descended from one another