8. BIOCHEMISTRY The chemistry of the carbon atom
Versatility of the carbon atom
Bonds readily to itself, forms chains, rings, single and double bonds
Hydrocarbons
Isomers
Polymers

10. I. Carbohydrates Sugars and their polymers CHO in a 1:2:1 ratio
An –OH group is attached to each C except one which is double bonded to Oxygen
Most common:
Triose 3C glyceraldehyde
Pentose 5C ribose
Hexose 6C glucose

12. A. Monosaccharides Simple sugars
C6H12O6 – glucose, fructose, galactose
Arrangement of individual atoms makes them different compounds
Glucose – hexose – building block for more complex sugars
Fructose – fruit sugar
Galactose – milk sugar

16. B. Disaccharides
2 monosaccharides joined by a glycosidic linkage through dehydration synthesis
Maltose = glucose + glucose (brewing beer)
Lactose = glucose + galactose (milk)
Sucrose = glucose + fructose (table sugar)

18. C. Polysaccharides
Polymer of a few hundred or thousand monosaccharides
2 important functions:
1. Energy storage (starch and glycogen)
2. Structural support (cellulose and chitin)
Starch = alpha linkage
Cellulose = beta linkage

24. II. LIPIDS Waxy or oily organic compounds
Nonpolar; CHO in no particular ratio
Fats, phospholipids, steroids
Functions:
Energy storage
Bio membranes
Chemical messengers
Insulation
Cushion vital organs

25. A. Fats Glycerol and 3 fatty acids Simple fat = triglyceride
Properties depend on the fatty acids that it is composed of
Saturated vs. unsaturated fatty acids

26. B. Phospholipids
Glycerol, fatty acids (2) and a phosphate group (negatively charged)
AMPHIPATHIC

27. C. Steroids
Lipids with 4 fused carbon rings with various functional groups attached
Amphipaathic
Cholesterol, hormones

32. III. PROTEINS
Polymers of amino acids
Amino acids are the monomers

34. III. PROTEINS cont’d
Amino acids can form covalent bonds with each other
20 AA in nature – each has a different “R” group
R groups can be
Polar
Nonpolar
special

41. III. PROTEINS Formation
Two amino acids form a peptide bond through dehydration synthesis
Peptide bond formed between acid group of one amino acid and and amino group of another
40 – 1,000 AA in MOST cellular proteins

43. PROTEINS Structure Primary – linear sequence of amino acids
Secondary – folding due to H bonds (weak forces) (alpha helix, beta pleated sheet)
Tertiary – more folding of helix due to hydrophobic/hydrophilic interactions of R groups
Quaternary – two or more chains held together by weak forces

47. PROTEINS Functions Membrane structure (integral and peripheral)
Enzymes (biological catalysts)
Motion (muscle contraction)
Energy (last resort)
Transport (hemoglobin)
Hormones (cellular control)
Regulation of gene function
Protection (immune system)

48. III. PROTEINS cont’d
Denaturing occurs when temperature or pH changes or through treatment with urea
3D structure is destroyed – no function
Primary structure is still intact; peptide bonds are strong covalent bonds that cannot be broken by change in pH, temp, etc

49. IV. NUCLEIC ACIDS
DNA and RNA, molecules which contain directions to make proteins; determine physical appearance, internal makeup, etc
Building blocks = nucleotides
Nucleotide = sugar (5C), phosphate and a nitrogenous base
In DNA, deoxyribose, phosphate, and one of four N bases (adenine, thymine, cytosine, guanine)

50. IV. NUCLEIC ACIDS cont’d
RNA = ribose, phosphate group, and one of 4 N bases (adenine, uracil, cytosine and guanine)
DNA = double helix; RNA single stranded
Over 100 million base pairs in one human DNA molecule
Base pairing rules
In DNA bases joined together by H bonds to make up rungs of ladder