Macro Molecules (Lesson 4)

Question 1

Main classes of biological molecules

Answer 1

Nucleic Acid, carbohydrates, lipids, and proteins.

Question 2

“The backbone”

Answer 2

All organic compounds contain carbon “the backbone” it can form large, complex, and diverse molecules.

Question 3

Why is carbon such a special element?

Answer 3

Electron configuration determines the kinds and number of bonds an atom will form with others atoms.

• can form 4 covalent bonds (bonds with up to 4 separate atoms + bond with any other C atoms)
• Most contain H/O but may contain other elements.

Question 4

Functional groups

Answer 4

Molecular components attached to that carbon, give molecule distinctive chemical properties to skeletons.

Question 5

Monomer

Answer 5

Single unit

Question 6

Polymer

Answer 6

Chain or ring of monomers (Chain repeated subnits)

Question 7

Building Chains (polymers)

Answer 7

A bond forms and water is released.

- Dehydration Synthesis (Condensation reaction): removes 1 water molecule, forming a new bond

Question 8

Breakdown of Chains (polymers)

Answer 8

Water is added and a bond is broken

-Hydrolisis of a polymer: adds a water molecule, breaking a bond.

Question 9

Carbohydrates

Answer 9

Sugars (simple/complex), broken down for energy in a process called cellular respiration.
- Energy in ATP (stored as long chains for short-term energy reserves in muscles and livers and animals)

Question 10

Function of Carbohydrates

Answer 10

1) Serve as source of energy

2) Provide structure/support

Question 11

Monosaccharides

Answer 11

One molecule of sugar (glucose is the most common)

Question 12

Disaccharides

Answer 12

2 linked monosaccharides (sucrose, lactose, maltose –> all isomers of eachother)

Question 13

Polysaccharides

Answer 13

Polymers of monosacharides

Question 14

Types of Carbohydrate

Answer 14

Storage:

1) Starch: Energy storage in plants (stored as ganules in plastic)
2) Glycogen: Energy storage in animals (granules in liver/cells)

Structural carbohydrate:

1) Cellulose: support in plants (woods), fiber
2) Chitin: found in fungal in cell walls/external skeleton of insects and other arthropods

Question 15

Herbivores Digestion System

Answer 15

Herbivores can’t produce enzymes to breakdown cellulose

- House bacteria in their digestive sysrem and the bacteria have enzymes to breakdown cellulose

Question 16

Lipids

Answer 16

Unifying feature of lipids is that they all have little or no affinity for water (high diverse in form and function)
- Neutral fats, Phospholipids, Steroids

Question 17

Neutral Fats

Answer 17

All are hydrophobic meaning that they are not soluble in water

Question 18

Function of Neutral Fats

Answer 18

1) Long-term energy reserves in fat tissue
2) Maintaining body temperature through insulation
3) Protection of vital organs from shock
4) Buoyancy

Question 19

Structure of Fats

Answer 19

Fat is constructed from 2 kinds of smaller molecules (1 molecule of glycerol and 1 to 3 molecules of fatty acids)

Question 20

Saturated Fat

Answer 20

Long chain saturated fattu acids stack well together to make solid forms at room temperature (not as healthy)

Question 21

Unsaturated Fat

Answer 21

Monosaturated and polyunsatured fatty acids do not stack well together beacuse they are bent. These are liquid are room temp
- double-bond

Question 22

Phospolipids

Answer 22

Major constituent of cell membrane

Question 23

Structure of Phospolipids

Answer 23

• 2 molecules to fatty acids
• 1 glycerol molecule
• 1 phosphate molecule
  Head: hydrophilic
  Tail: Hydrophobic

Question 24

Function of Steroids

Answer 24

1) Cell membrane (cholesterol)
2) Vitamins
3) Hormones

Question 25

Structure of Steroids

Answer 25

- Made from Sterol, multiple rings of carbon atoms | - Different molecules are made in our bodies from sterol

Question 26

Protein

Answer 26

The workhorses in the cell. They make up 50% of the organic matter in a typical animal body. Made of amino acids (monomers), they all have basic skeleton.

Question 27

Function of Protein

Answer 27

1) Transport proteins -> coordinate movement 2) Enzymes -> catalyze specific reactions in cells 3) Protein hormones -> acts as messengers 4) Receptors -> Receive/Relay

Question 28

Amino Acids

Answer 28

They contain carbon, hydrogen, oxygen, nitrogen, some sulfer. Structure: 2 functional groups + 1 variable group (20 common aa)

Question 29

Polypeptide

Answer 29

Chain of amino acids created by dehydration synthesis, repeating structure of atoms from the polypeptide backbone with the side chains coming out of it.

Question 30

Protein Shapes

Answer 30

1) Primary Structure 2) Secondary Structure 3) Tertiary Structure 4) Quaternary Structure

Question 31

Primary Structure

Answer 31

Specefic and unique sequence of animo-acids that composes polypeptide. Order of AA is determined by the nucleotide sequence of the gene that encodes the protein

Question 32

Sickle Cell Anemia

Answer 32

Substitution of 1 cell in primary structure; blood cell dont have the same shape + cant carry same amount oxygen (not healthy red blood cell)

Question 33

Secondary Structure

Answer 33

The coiling and folding of a sequence of AA withing a polypeptide (due to hydrogen bonding forming regular intervals) + H-bonds forming between amino/carboxyl group

Question 34

Alpha helix

Answer 34

Delicate coil held together by H-bonds (happens on 4th) - Common in fibrous protein (hair/wool/nails) - H-bonds can be broken which allows the fibersto sketch under tension - Once released, the fibers can recoil/can reform.

Question 35

Beta Pleated sheet

Answer 35

H-bond between regions in polypeptides backbone; hold neighboring strands of sheet together. (chains lying, anti parallel); make up care of globular proteins

Question 36

Tertiary structure

Answer 36

The forces holding a single polypeptide together. Ex: H-bonds, ionic bonds, disulfide bridges, etc.

Question 37

4 main interactions between R groups

Answer 37

1) Hydrogen Bonds: bonds involving H 2) Ionic Bonds: results from ions + / - charges 3) Hydrophobic Interactions: Non-water soluable molecules interacting with 1 another 4) Covalent Bonds/Disulfide Bonds: Equal sharing of electrons between sulfide groups on AA.

Question 38

Quaternary Structure

Answer 38

Formed by the interactions among the polypeptide chain that comprise the protein. The fusion of 2 or more polypeptides into 1 functional macromolecules.

Question 39

Hemoglobin

Answer 39

Globular protein wit 4 polypeptide subnits

Question 40

Collagen

Answer 40

Fibrous protein consisting of 3 helical polypeptides coiled together to create 1 ropelike structure

Question 41

Monomerie

Answer 41

Proteins made of a single polypeptide chain (no quaternary structure)

Question 42

Oligomerie

Answer 42

2 or more polypeptide chains

Question 43

Denaturation

Answer 43

Proteins are influenced by their environment/can unravel or change shape. (Can be temporary) -Breakdown of proteins -Distrupts alpha-helix/beta sheets -> random shape (doesn't break the peptide bonds)

Question 44

Ribosomes

Answer 44

Displays quaternary structure and uses RNA to make other proteins and made in nucleus.