1. Macromolecules

2. Four major classes of organic molecules
Carbohydrates
Lipids
Proteins
Nucleic acids
All are CARBON-BASED

3. Smaller components strung together to make large molecules
Monomers – individual building blocks
Polymers – large molecules composed of repeating units (monomers)

4. carbohydrates
Composed of C, H, and O in a 1:2:1 ratio
Names often end in –ose
Function – energy source and short-term energy storage

5. Monomers of carbohydrates
Monosaccharides (also called simple sugars)
Usually look like pentagons or hexagons

6. Polymers of carbohydrates
Polysaccharides – chains of monosaccharides (most often glucose)

7. lipids
Composed of C, H, and O
Include fats, waxes, oils, steroids
Non-polar - hydrophobic

8. Functions of lipids
Long-term energy storage
Component of the cell membrane (phospholipid bilayer)
Hormones (chemical messengers)

9. Triglycerides (most common form)
Consist of a glycerol backbone and 3 fatty acid chains

10. Saturated vs. unsaturated fats
Saturated – no double bonds in the fatty acid chain (carbon molecules are saturated with hydrogen)
Unsaturated – one or more double bonds in the fatty acid chain

11. Saturated vs. unsaturated fats
Double bonds in the fatty acid chains cause “kinking” – molecules cannot pack as tightly together
Saturated fats – solid at room temp
Butter, lard, animal fats
Unsaturated – liquid at room temp
Oils, plant fats

12. Proteins Composed of C, H, O, and N
Functions include transport (hemoglobin), regulate chemical reactions (enzymes), let things in/out of cells (membrane proteins), fight infection (antibodies), movement (muscle filaments), chemical messengers (hormones), give structure (keratin in nails, collagen in skin)

13. Monomers of proteins
Amino acids – composed of a central carbon surrounded by an amine group, a carboxyl group, a hydrogen, and a variable R group

14. Monomers of proteins
Amino acids – 20 different R groups give each amino acid its own properties (polarity, acidity, etc.)

15. Polymers of proteins
Amino acids are linked together by peptide bonds to form polypeptides which then fold to become functional proteins

16. Levels of protein structure
Primary structure – sequence of amino acids
Secondary structure – hydrogen bonds between nearby amine groups and carboxyl groups create alpha helix and beta pleated sheets

17. Levels of protein structure
Tertiary structure – R groups of amino acids form bonds with each other to give the protein a very specific 3D shape

18. Levels of protein structure
Quaternary structure – some proteins are done at tertiary, but some have another level of organization in which two or more polypeptides form bonds between R groups of their amino acids to join them together.
Can also include non-protein elements
Ex. Iron in hemoglobin

19. Levels of protein structure
Each level depends on the previous levels – if you change the primary structure, the secondary, tertiary, and quaternary structures are altered

20. Nucleic acids
Composed of C, H, O, N, and P
Include DNA and RNA
Store and transmit genetic information

21. Monomers of nucleic acids
Nucleotides – consist of a 5 carbon sugar (ribose or deoxyribose), a phosphate, and a nitrogenous base

22. Polymers of nucleic acids
DNA (double stranded) and RNA (single stranded)