Macromolecules

Question 1

Glycogen: animal storage

Answer 1

stored as granules in muscle or liver. very branched, dosen’t last long

Question 2

how are starch and cellulose different?

Answer 2

the different placement of the hydroxyl groups in glucose results in different shapes (

Question 3

Polysaccharide

Answer 3

long chains of carbohydrate molecules composed of several smaller monosaccharides

Question 4

-saccharide

Answer 4

group that incorporates starch, cellulose, and sugar

Question 5

Lipids

Answer 5

hydrophobic molecules
- fats
- phospholipids
- steroids

Question 6

Fat: triglyceride

Answer 6

glyceride backbone, 3 tails called fatty acids (storage contain a lot of energy)

Question 7

Saturated v unsaturated

Answer 7

saturated:
no double bonds
max # of H+ are attached to carbons
NO kinks in chain
ex. butter

unsaturated:
one or more double bonds (creates kinks)
chain has kinks, makes it more fluid
ex. olive oil

Question 8

Phospholipids

Answer 8

two fatty acid tails + a phosphate head
makes phosphate polar (hydrophobic head, hydrophilic tail)
very important to cell membrane

Question 9

Steroids

Answer 9

whole class of chemical messengers
4 lipid rings fused together

Question 10

hydrogenated

Answer 10

means add more hydrogens
ex. hydrogenated vegetable oil –> is solid at rom temp because more hydrogens have been added leading to less tail kinks (stack better)

Question 11

Enzymes

Answer 11

speed up reactions

Question 12

storage

Answer 12

source of amino acids for use later

Question 13

Transport

Answer 13

facilitate movement of a substance within body and or cells

Question 14

Receptors

Answer 14

recognize other molecules (pick up signaling between nerve cells)

Question 15

Proteins!

Answer 15

Enzymes
storage
defense
transport
hormones
receptors
movement
structure

Question 16

what is a protein?

Answer 16

polymer of amino acids, linked by peptide bonds to form polypeptide

Question 17

polypeptide

Answer 17

many amino acids connected

Question 18

peptide bond

Answer 18

covalent bond between carboxyl group and amine group

Question 19

Amino acids

Answer 19

20 of them, they differ by their R group

Question 20

protein structure

Answer 20

properties of amino acids in the polypeptide bond lead to different shapes of proteins
- fold according to charges in chemical reactions
- shape os critical to function

Question 21

Primary structure

Answer 21

sequence of amino acids. dictates secondary and tertiary structure

Question 22

Secondary structure

Answer 22

regions stabilized by hydrogen bonds between the polypeptide chain
- different regions within the polypeptide fold differently due to hydrogen bonding
two types:
alpha helix - a coiled structure
beta helix - chains lying side by side (sheet)

Question 23

Tertiary structure

Answer 23

3D shape by interacting interactions with side chains
- may cluster according to polarity: hydrophobic or hydrophilic
Reinforced by…
- hydrogen bonding
- ionic bonds
- disulfide bridges ( type of covalent bond )

Question 24

Quaternary structure

Answer 24

overall 3-D protein structure of multiple polypeptide subunits

Question 25

Breaking proteins

Answer 25

pH
salt concentration
temperature
other environmental factors
- damage is reversible as long as it isn’t to the primary structure!!

Question 26

Denature

Answer 26

when a protein loses its particular shape, it will not function properly
- breaks weak bonds (hydrogen bonds) causing the proteins shape to start to fall apart

Question 27

Nucleic Acids

Answer 27

polymers of nucleotides
2 types –> DNA and RNA

Question 28

what is a nucleotide?

Answer 28

• nitrogenous base (contains nitrogen)
• 5 carbon sugar (pentose)
• one or more phosphate groups

Question 29

Nitrogenous bases

Answer 29

Pyrimidines: C,T (in DNA), U (in RNA)
Purines: A, G

Question 30

Mutations

Answer 30

result in changes in protein expression, raw material evolution