Chapter 5 Reading Quiz. Splitting water. What does “hydrolysis” literally mean? What element composes the backbone of the 4 macromolecules? What subunits come together to make a protein? List the 3 other macromolecules. What is the main function of DNA?. Carbon!. Amino acids.
Unity – there are only 40 – 50 monomers used to make all macromolecules
Diversity – new properties emerge when these monomers are arranged in different ways…leading to the diversity of life
Condensation unity and diversity.
Polymerization reaction where monomers are covalently linked, removing a water molecule
Remove H2O molecule
Reaction process that breaks covalent bonds between monomers by adding water molecules
Add H2O molecule 3. Describe how covalent linkages are formed (condensation) and broken (hydrolysis) in organic polymers.
Carbohydrates are classified by the number of simple sugars
They are organic molecules made of sugars and their polymers
2. The size of the carbon skeleton varies from 3-7 carbons
3. Spatial arrangement around asymmetric carbons may vary (ex: enantiomers)
4. In aqueous solutions, many simple sugars form rings. (chemical equilibrium favors ring structures)
Glycosidic linkage – the covalent bond formed by a condensation reaction between 2 sugar monomers
Sugar + Sugar Big Sugar
(monosaccharides) (glycosidic (disaccharide)
2. Structural support – in the form of cellulose and chitin
Glucose monomers in α configuration
-OH group is BELOW ring’s plane
α 1-4 linkage
Glucose monomers in β configuration
-OH group is ABOVE ring’s plane
β 1-4 linkage 8. Distinguish between the glycosidic linkages found in starch and cellulose.
10. Describe the unique properties, building block molecules and biological importance of the three important groups of lipids: fats, phospholipids and steroids.
Fats – made with glycerol, a 3 carbon alcohol and a fatty acid (carboxylic with a hydrocarbon tail)
Phospholipids – made with a glycerol, 2 fatty acids, a phosphate group, and a small chemical group
Steroids – are lipids that have 4 fused carbon rings with various functional groups attached
- precursor to sex hormones and bile acids
- common in cell membranes
Ester linkage –
-OH + -COOH
Saturated Fats and biological importance of the three important groups of lipids: fats, phospholipids and steroids.
No double bonds between carbons in tail
Has maximum number of hydrogens
Solid at room temperature – most animal fats
One or more double bonds in tail
Tail kinks at C=C so molecules do not pack closely enough to solidify
Liquid at room temperature – most plant fats
12. Distinguish between saturated and unsaturated fat,and list some unique emergent properties that are a consequence of these structural differences.
Proteins – a macromolecule that consists of one or more polypeptide chains folded and coiled into specific conformations
2. Storage of amino acids
3. Transport (hemoglobin)
4. Signaling (chemical messengers)
5. Cellular response to chemical stimuli (receptor proteins)
6. Movement (contractile proteins)
7. Defense against foreign substances & disease-causing organisms (antibodies)
8. Catalysis of biochemical reactions (enzymes)
14. List and recognize four major components of an amino acid, and explain how amino acids may be grouped according to the physical and chemical properties of the side chains.
1. Hydrogen atom
2. Carboxyl group (-COOH)
3. Amino group (-NH2)
4. Variable ‘R’ group (specific to each amino acid)
- the properties of the side chain determine the uniqueness of each amino acid
Peptide bond = the covalent bond formed by a condensation reaction that links the carboxyl (-COOH) group of one amino acid to the amino (-NH2) group of another.
In a laboratory…
2. Beta pleated sheet
Weak Interactions and explain the role of hydrogen bonds in maintaining the structure.
Hydrogen bonding between polar side chains
Ionic bonds between charged side chains
Hydrophobic interactions between nonpolar in interior
Disulfide bridges between 2 cysteine monomers brought together by folding
Reinforces conformation 19. Explain how weak interactions and disulfide bridges contribute to tertiary protein structure.
Collagen and explain the role of hydrogen bonds in maintaining the structure.
Fibrous protein with 3 helical polypeptides supercoiled into a triple helix
Four subunits grouped together (2 α chains and 2 β chains) 20. Using collagen and hemoglobin as examples, describe quaternary protein structure.
Nucleic acids –
- directions for replication
- information to run all cell activity
- make up the genes for protein synthesis
(the ‘brain’ for making anything)
- ribose, deoxyribose
2. Phosphate – attached to the 5th carbon of the sugar
3. Nitrogenous base – pyrimidines & purines
Pyrimidine describe how these monomers are linked together to form a nucleic acid.
six-membered ring made up of carbon and nitrogen atoms
Ex: cytosine (C)
thymine (T) – DNA
uracil (U) – RNA
five-membered ring fused to a six-membered ring
Ex: Adenine (A)
25. Distinguish between a pyrimidine and a purine.