Macromolecules Flashcards

1
Q

What are monosaccharides?

A

Simplest sugars containing only one carb.

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2
Q

What are disaccharides?

A

2 linked monosaccharide units.

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3
Q

What are oligosaccharides?

A

3 or more linked monosaccharide units.

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4
Q

What are polysaccharides?

A

100s and thousands of monosaccharide units that are joined.

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5
Q

What configurations do monosaccharides come as?

A

Alpha or Beta

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6
Q

What are homopolysaccharides?

A

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

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7
Q

What are heteropolysaccharides?

A

Polysaccharides containing more than one monosaccharide unit.

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8
Q

What structural significance does glycogen have?

A

It is branched

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9
Q

Why is it useful to have glycogen branched?

A

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

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10
Q

What is the importance of heteropolysaccharides in bacterial cell walls?

A

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

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11
Q

What can degrade peptidoglycans?

A

Lysozymes

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12
Q

What is the significant function of glycoproteins and glycolipids?

A

Within cell membrane

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13
Q

What are amino acids?

A

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

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14
Q

How are amino acids classified?

A

According to their R group.

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15
Q

What are polypeptides?

A

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

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16
Q

What are the four structures of protein?

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quaternary
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17
Q

What is a typical primary protein structure?

A

Amino acids linked with a covalent bond

18
Q

What is a typical secondary protein structure?

A

Coiling into alpha helix or beta sheets

19
Q

Which secondary coiled structure is considered “simpler”?

A

Alpha helix

20
Q

What are nucleic acids made out of?

A

Monomers called nucleotides

21
Q

What is a simple nucleotide structure?

A
  1. Five carbon sugar
  2. Phosphate group
  3. Nitrogenous base
22
Q

What binds complementary DNA strands?

A

Hydrogen bond

23
Q

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

A

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

24
Q

What is the characteristic kink represents?

A

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

25
Q

What are phospholipids?

A

Molecules with phosphate head and a lipid tail

26
Q

What are sphingolipids?

A

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

27
Q

How do we create an active enzyme (holoenzyme)?

A

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

28
Q

How do enzymes work?

A

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

29
Q

What enables an enzyme to bind specifically to its substrate?

A

Complimentary shaping of the active site

30
Q

What type of kinetics do un-regulated enzymes follow?

A

Michaelis Mente kinetics

31
Q

What does affinity mean?

A

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

32
Q

What are the two types of non Regulatory Enzyme inhibition?

A
  1. Reversible (Weak covalent bonding)

2. Irreversible (Strong Covalent bonding)

33
Q

What is competitive inhibition?

A

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

34
Q

What is non-competitive inhibition?

A

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

35
Q

What is un-competitive inhibition?

A

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

36
Q

What are irreversible inhibitors?

A

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

37
Q

What is feedback inhibition?

A

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

38
Q

What cellular processes regulate controlled enzyme activity?

A
  1. Allosteric control
  2. Covalent modification
  3. Zymogens
  4. Isozymes
39
Q

What is allosteric enzyme regulation?

A

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

40
Q

What is a covalent modification?

A

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

41
Q

What is zymogen modification?

A

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

42
Q

What are isozymes?

A

Enzyme with same catalytic function but different kinetics.