1. Functional Groups and Macromolecules
Biochemistry
Functional Groups
and
Macromolecules

2. Biochemistry
Part 2:
Macromolecules

3. Polymers are MADE/BROKEN a lot in biology
Macromolecule = biomolecule
Molecule of life
Most macromolecules are polymers, built from monomers
Polymer = “chain”
Monomer = single “link” in polymer chain
Polymers are MADE/BROKEN a lot in biology

4. Putting Polymers Together
Covalent monomers
Formed by condensation reaction
aka- dehydration reaction
One monomer provides a -OH group while the other provides a –H to form a H2O
Ex: making proteins, DNA, etc.  BIOSYNTHESIS

5. Breaking Apart Polymers
Hydrolysis:
bonds between monomers are broken by adding H2O
Ex: breaking apart DNA, protein  digestion

6. There are 4 macromolecules needed for life

7. 1. Carbohydrates LOTS of: Has one carbonyl group
a. Monosaccharides
LOTS of:
-OH’s
Has one carbonyl group
Needed in cellular respiration
raw material for
amino acids and fatty acids

8. 2 FORMS of Glucose
α Glucose
β Glucose
Structural iosmers!!!

9. Carbohydrates cont’d b. Disaccharides glycosidic linkage
covalent bond between 2 monosaccharides
covalent bond by dehydration reaction
Ex: Sucrose (table sugar)
most common disaccharide
1-2 link
1-4 link

10. Plus 1 water molecule b/c DEHYDRATION RXN
Common Disaccharides
Glucose + Glucose = Maltose (found in beer)
USES a 1-4 Carbon glycosidic linkage
**Glucose + Fructose = Sucrose (table sugar…YUM!)
USES a 1-2 Carbon glycosidic linkage
Glucose Galactose = Lactose (milk sugar)
Plus 1 water molecule b/c DEHYDRATION RXN

11. Carbohydrates cont’d still!!
c. Polysaccharides
Function #1
SHORT TERM Energy Storage!!!!
Starch (PLANTS)
Chains of glucose
Glycogen (ANIMALS)
Stored in liver

12. Carbohydrates cont’d still!!
c. Polysaccharides (con’t)
Function #2
Structural/Support!!!!
Cellulose (aka –Fiber… to humans)
most abundant compound in world
Wood and cell walls
Chitin
Insect exoskeletons
Cell walls of fungi
Surgical thread

13. 2. Lipids Not polymers Instead glycerol + fatty acid
Includes fats, phospholipids, steroids
Hydrophobic (NON-POLAR)
Non-polar C-H bonds in fatty acid ‘tails’
Ester linkage: covalent bonds in lipids

14. Function of Lipids Main Function
Lipids= long term energy storage like carbs but carbs = short-term usage
Other functions:
Insulation
Protection (membranes)
Chemical signals

15. 3 different types of Lipids
a. Fats
Triacyglycerol (triglyceride)
Saturated vs. unsaturated fats
single vs. double bonds

16. unsaturated
Saturated

17. Lipids cont’d

18. b. Phospholipids 2 fatty acids instead of 3 1 phosphate group
‘Tails’ hydrophobic
NON-POLAR
‘Heads’ hydrophilic
POLAR

19. b. Phospholipids
Bilayer
double layer in cell membranes

20. c. Steroids Lipids with 4 or 5 fused carbon rings Helps make
animal membranes
cell signaling/messaging
Ex: cholesterol, cell membranes, precursor for other steroids, sex hormones

21. Waxes – 1 fatty acid chain; very hydrophobic
Another Type of Lipid
Waxes – 1 fatty acid chain; very hydrophobic

22. #3. Proteins Monomer = Amino Acids
Center carbon, carboxyl group, amino group
Some amino acids are polar or charged, some nonpolar
20 amino acids = many combo’s; R group makes them different

23. R group characteristics
Proteins (con’t)
R group characteristics
Some are:
polar (hydrophilic)
nonpolar (hydrophobic)
Acidic
Basic
ALL proteins have a 3D shape (called its conformation)
Form polypeptides
peptide bonds (covalent bond) are created

24. Peptide Bonds
Amino acids connected by peptide bond (covalent) bonds via dehydration

26. Proteins have 3 (and sometimes 4) for LEVELS of conformation
Proteins (con’t)
Proteins have 3 (and sometimes 4) for LEVELS of conformation

27. i. Primary Structure **Uses peptide bonds Conformation:
Linear structure of linked together amino acids
each type of protein has unique primary structure of amino acids
**Uses peptide bonds

28. ii. Secondary Structure
Conformation:
coils & folds
Uses hydrogen bonds
Alpha Helix:
coiling
Pleated Sheet:
parallel

29. iii. Tertiary Structure
Conformation:
The 3D structure
Involves R groups bonding together
R group = specific to EACH amino acid
hydrophobic
disulfide bridges
hydrogen bonds
ionic bonds
Van der Waals

31. iv. Quaternary Structure
Conformation:
When 2 or more polypeptides chains combine into 1 macromolecule
SAME bonds used as 3° structures
Examples:
Collagen (connective tissue)
Hemoglobin (blood protein)

33. DNA  RNA  protein  trait
4. Nucleic Acids
a. Deoxyribonucleic acid (DNA)
Holds genetics information
B. Ribonucleic acid (RNA)
Carries genetics information
DNA  RNA  protein  trait
(called Central Dogma of Biology)
Made of polymers of nucleotides
Nucleotide
nitrogen base, pentose sugar & PO43-
Nitrogenous bases:
pyrimidines (small)= cytosine thymine, uracil
Purines (big)= adenine, guanine

34. SMALL BASES
LARGE BASES

35. SMALL BASES
U instead of T
RNA
LARGE BASES

37. **Monomer of a nucleic acid (DNA or RNA)
Nucleotide
**Monomer of a nucleic acid (DNA or RNA)
HAS 3 PARTS:
Pentose Sugar
(5 carbons)
**ribose (RNA)
**deoxyribose (DNA)
2. Nitrogen base
3. Phosphate group (PO4-3)

40. Nucleic Acids (con’t) Polynucleotide Hooks together phosphate + sugar
Uses Phosphodiester
linkages
Covalent bonds in DNA and RNA
Hooks together phosphate + sugar

41. AATCGAT TTAGCTA Nucleic Acids Inheritance based on DNA replication
Double helix
Watson & Crick – 1953
H bonds
between paired bases
Also uses van der Waals forces
A to T & C to G pairing
Complementary
AATCGAT
TTAGCTA