Biochemistry Flashcards

1
Q

4 types of large biological molecules in body

A
  1. Protein
  2. Carbohydrates
  3. Lipid
  4. Nucleic Acid
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2
Q

Which one of the four large biological molecules is distinctively different from the others? How?

A

Lipid, all others are polymers

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3
Q

Reaction of monomers joining to form polymer

A

Condensation / dehydration

2 mononers join, lose 1 water molecule

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4
Q

Reaction of polymer dissembling into monomers

A

Hydrolysis

adding of water, H on one end, OH on another end

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5
Q

2 Classes of carbohydrates based on location of carbonyl group (C=O) group

A
  1. Aldoses - carbonyl at end of chain

2. Ketoses - carbonyl in middle of chain

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6
Q

Name of bond between monosaccharides

A

Glycosidic linkage

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7
Q

Major difference between storage polysaccharides in plant and animal? What is the purpose of that?
(plant: starch, animal: glycogen)

A

Greater level of branching in glycogen –> need multiple enzymes to be broken down –> slow down rate of breaking

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8
Q

Monomers of carbohydrates

A

monosaccharide

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9
Q

Monomers of protein

A

amino acid

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10
Q

pKa of carboxyl group

How would it be changed?

A

pKa: 4
<4: more COOH
>4: more COO-

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11
Q

pKa of amino group

How would it be changed?

A

pKa: 9
<9: more NH3+
>9: more NH2

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12
Q

Name of the state when 2 ions are present in the amino acid? (NH3+ & COO-) When would it occur?

A

Zwitter ion

4 < pH < 9

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13
Q

Name of bond joining amino acids together

A

Peptide bond

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14
Q

Word describing amino acids with 4 different substituents

A

chiral

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15
Q

Name for isomers that are different in spatial arrangement (mirror images)

A

enantiomers

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16
Q

2 models for protein

A
  1. Ribbon Model

2. Space-filling model

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17
Q

How many different amino acids are there?

A

20

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18
Q

From which end is an amino acid sequence numbered from?

A

amino end (with NH2/NH3+)

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19
Q

3 types of secondary structure in protein

A

a helix
B sheet
random coil

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20
Q

What is secondary structure stabilized by?

A

hydrogen bonds
(a helix: between nearby residues)
(B sheet: between carbonyl group from one amino acid and amino group from another)

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21
Q

What is tertiary structure of protein resulted from?

A

Non-covalent interactions between amino acids and side chains

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22
Q

How many polypeptides are there in myoglobin and haemoglobin respectively?

A

myoglobin: 1
haemoglobin: 4

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23
Q

What do homologous proteins share? Give an example of homologous proteins.

A

Similar primary, secondary & tertiary structure

e.g. myoglobin & haemoglobin

24
Q

How many polypeptides are in haemoglobin? How are they different?

A

4.

2 alpha chains, 2 Beta chains

25
Q

Where is the mutation in sickle cell disease? What is the mutation?

A

in Beta chain
glutamate –> valine
negatively charged –> non-polar

26
Q

What happens in sickle-cell haemoglobin?

A

Aggregation: mutated deoxyhaemoglobin gets attracted and locked into one another –> form long & insoluble fibres –> greatly reduce capacity to carry oxygen

27
Q

How is insulin activated?

A

Proteolytic (enzyme) cleavage breaks proinsulin into active insulin
with 2 polypeptide chains held together by strong disulfide bonds

28
Q

What is globular protein? And what are its characteristics?

A

Soluble proteins:

  1. hydrophobic amino acids located inside core of protein
  2. hydrophillic amino acids on surface of protein
29
Q

Is collagen soluble in water?

A

No, it is fibrous and insoluble in water.

30
Q

Major function of collagen?

A

Provide mechanical strength to connective tissue

31
Q

What are the inactive and active forms of collagen called?

A

inactive: procollagen
active: tropocollagen

32
Q

How is collagen activated?

A

By procollagen peptidase. It breaks the peptide bond linking the loose ends at the amino group terminal and carboxyl group terminal.

33
Q

How many polypeptides are there in collagen? Give an important characteristic of them.

A

3, they intertwine with each other.

34
Q

What is the structure of collagen called?

A

triple-helix

35
Q

What is the significance of vitamin C in collagen?

A

Vitamin C activates prolyl-4-hydroxylase (enzyme)
prolyl-4-hydroxylase catalyzes formation of hydroxypoline from proline ring -> form more hydrogen bonds -> strengthening collagen

36
Q

What is a disulfide bond? Between which amino acid would it be formed?

A

strong covalent bond between 2 sulfides.

Formed between cysteine.

37
Q

What happens to collagen in osteogenesis imperfecta?

A

glycine (smallest amino acid) at core of the triple-helix is replaced by cysteine –> disrupt helical arrangement and hydrogen bonds –> weakened triple-helix

38
Q

6 steps in collagen biosynthesis:

A
  1. Single strands of polypeptides are formed
  2. Hydroxylation (adding of hydroxy group) of proline and lysine side chains
  3. Triple-helix is formed
  4. Procollagen is converted to tropocollagen by procollagen peptidase
  5. Bundles form (associating layers)
  6. Cross links form (enzyme attach individual collagen molecules together)
39
Q

3 types of biologically important lipids

A
  1. Fats
  2. Phospholipids
  3. Steroids
40
Q

What are fats constructed from?

A

Glycerol and fatty acids

41
Q

How are the fatty acids attached to the glycerol?

A

Dehydration –> Ester Linkage

42
Q

Another name for fat

A

triglyceride

43
Q

Functions of fat

A
  1. Energy storage
  2. Protect vital organs
  3. Insulate body
44
Q

Composition of phospholipid

A

2 fatty acids and 1 phosphate group attached to a glycerol

45
Q

Where does protein synthesis occur?

A

In ribosomes

46
Q

What controls protein synthesis?

A

mRNA

47
Q

Monomer of nucleic acid

A

nucleotides

48
Q

Polymer of nucleic acid

A

polynucleotides

49
Q

2 Major types of nitrogenous bases

A
  1. Pyrimidines: 6-membered ring (C, T, U for RNA)

2. Purines: 6-membered ring fused to a 5-membered ring (G, A)

50
Q

What is the backbone of polynucleotides called? And the appendages?

A

Sugar-phosphate backbone

Appendages: nitrogenous bases

51
Q

How many polynucleotides are there in DNA?

A

2 polynucleotides

52
Q

How are the 2 polynucleotides arranged?

A

in double helix, with backbones running antiparallel to each other

53
Q

Name for spontaneous reaction with net release of energ

A

Exergonic reaction

54
Q

Name for non-spontaneous reaction with net absorb of energy

A

Endergonic reaction

55
Q

3 Steps in cellular respiration

A
  1. Glycolysis
  2. Citric acid cycle
  3. Oxidative phosphorylation