Macromolecules

Question 1

What are monosaccharides?

Answer 1

Simplest sugars containing only one carb.

Question 2

What are disaccharides?

Answer 2

2 linked monosaccharide units.

Question 3

What are oligosaccharides?

Answer 3

3 or more linked monosaccharide units.

Question 4

What are polysaccharides?

Answer 4

100s and thousands of monosaccharide units that are joined.

Question 5

What configurations do monosaccharides come as?

Answer 5

Alpha or Beta

Question 6

What are homopolysaccharides?

Answer 6

Polysaccharides containing a single monosaccharide unit, e.g glycogen.

Question 7

What are heteropolysaccharides?

Answer 7

Polysaccharides containing more than one monosaccharide unit.

Question 8

What structural significance does glycogen have?

Answer 8

It is branched

Question 9

Why is it useful to have glycogen branched?

Answer 9

Because then, separate brunches can be broken down for energy much more efficiently

Question 10

What is the importance of heteropolysaccharides in bacterial cell walls?

Answer 10

They are crucial structural components and are cross-linked with other compounds via peptidoglycans

Question 11

What can degrade peptidoglycans?

Answer 11

Lysozymes

Question 12

What is the significant function of glycoproteins and glycolipids?

Answer 12

Within cell membrane

Question 13

What are amino acids?

Answer 13

Amino acids are a combination of an amine group (NH2) and a carboxyl group.

Question 14

How are amino acids classified?

Answer 14

According to their R group.

Question 15

What are polypeptides?

Answer 15

They are chains of amino acids that are joined together by a peptide bond.

Question 16

What are the four structures of protein?

Answer 16

1. Primary
2. Secondary
3. Tertiary
4. Quaternary

Question 17

What is a typical primary protein structure?

Answer 17

Amino acids linked with a covalent bond

Question 18

What is a typical secondary protein structure?

Answer 18

Coiling into alpha helix or beta sheets

Question 19

Which secondary coiled structure is considered “simpler”?

Answer 19

Alpha helix

Question 20

What are nucleic acids made out of?

Answer 20

Monomers called nucleotides

Question 21

What is a simple nucleotide structure?

Answer 21

1. Five carbon sugar
2. Phosphate group
3. Nitrogenous base

Question 22

What binds complementary DNA strands?

Answer 22

Hydrogen bond

Question 23

What is the main storage method of lipids in adipose tissue?

Answer 23

Combine a glycerol molecule with a fatty acid to form a triacylglycerol.

Question 24

What is the characteristic kink represents?

Answer 24

Kink is present in unsaturated fats and represents a carbon double bond

Question 25

What are phospholipids?

Answer 25

Molecules with phosphate head and a lipid tail

Question 26

What are sphingolipids?

Answer 26

They are lipids composed of a polar head group and two nonpolar tails.

Question 27

How do we create an active enzyme (holoenzyme)?

Answer 27

Apoenzyme + a prosthetic group (such as co-factors or co-enzymes)

Question 28

How do enzymes work?

Answer 28

By using their electron-rich active sight they are able to lower the activation energy in order to break down certain molecules.

Question 29

What enables an enzyme to bind specifically to its substrate?

Answer 29

Complimentary shaping of the active site

Question 30

What type of kinetics do un-regulated enzymes follow?

Answer 30

Michaelis Mente kinetics

Question 31

What does affinity mean?

Answer 31

It is a rate of binding between substances. Easily speaking Low Km = High Affinity, meaning it needs little substrate concentration to be effecient.

Question 32

What are the two types of non Regulatory Enzyme inhibition?

Answer 32

1. Reversible (Weak covalent bonding) | 2. Irreversible (Strong Covalent bonding)

Question 33

What is competitive inhibition?

Answer 33

Inhibition process, in which inhibitor and substrate compete for the active site.

Question 34

What is non-competitive inhibition?

Answer 34

When the inhibitor binds away on a different site of the enzyme and this changes the shape of the active site.

Question 35

What is un-competitive inhibition?

Answer 35

The inhibitor binds only after the substrate has bound to the active site.

Question 36

What are irreversible inhibitors?

Answer 36

Inhibitors that either binds or destroys a functional group on the enzyme.

Question 37

What is feedback inhibition?

Answer 37

When end product inhibits the function of Enzyme 1 in the metabolic chain.

Question 38

What cellular processes regulate controlled enzyme activity?

Answer 38

1. Allosteric control 2. Covalent modification 3. Zymogens 4. Isozymes

Question 39

What is allosteric enzyme regulation?

Answer 39

Enzyme activity changes through the binding of the modulator. This may Increase or Decrease the activity of the enzyme. Non covalent/ reversible regulation.

Question 40

What is a covalent modification?

Answer 40

It is when the covalent bonding of modifying groups to enzyme produces inactive or active forms of the enzyme. Covalent / reversible inhibition.

Question 41

What is zymogen modification?

Answer 41

Precursor of active enzymes. Need a structural change to work.

Question 42

What are isozymes?

Answer 42

Enzyme with same catalytic function but different kinetics.