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Biotechnology Mid Term > CH3 | Proteins (1/2) > Flashcards

CH3 | Proteins (1/2) Flashcards

1
Q

Amino acids are the building blocks of…

A

proteins.

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2
Q

How many naturally occurring amino acids are there?

A

20.

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3
Q

The common structural features of amino acids are…

A

amino group (-NH2), carboxylate (-COOH) and hydrogen bonded to the same carbon atom.

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4
Q

Amino acids differ in their…

A

R group.

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5
Q

In the amino acid, the amino group is..

A

basic.

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6
Q

In the amino acid, the carboxylate group is…

A

acidic.

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7
Q

Protein primary structure is the exact order of…

A

amino acids in the chain.

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8
Q

The primary sequence determines the protein’s…

A

final fold and function.

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9
Q

Any change in primary sequence changes the…

A

entire protein.

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10
Q

What type of bond maintains the primary structure of a protein?

A

Covalent, peptide bonds.

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11
Q

Peptide bonds occur between which two groups of adjacent amino acids?

A

Amino and carboxyl.

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12
Q

Intramolecular bonding refers to…

A

bonds that occur within the atoms of the SAME molecule.

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13
Q

Intermolecular bonding refers to…

A

bonds that occur between ADJACENT MOLECULES.

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14
Q

Secondary structure refers to local folded structures within a polypeptide due to interactions between…

A

atoms of the backbone (without R group).

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15
Q

The most common secondary structures are…

A

α helix and β pleated sheet.

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16
Q

The α helix is stabilized by what type of bonds?

A

Hydrogen bonds.

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17
Q

Hydrogen bonds in α helix occur between which groups?

A

Amide (>N-H) and carbonyl (>C=O) groups.

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18
Q

An amide and carbonyl group that are hydrogen-bonded are how far apart on the amino acid chain?

A

4 amino acids.

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19
Q

How many amino acids are there in every twist of the α-helix?

A

3.6 amino acids.

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20
Q

Naturally occurring α-helices in proteins are…

A

right-handed.

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21
Q

An α-helix can be formed from how many polypeptide chains?

A

One (single chain).

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22
Q

Hydrogen bonds in α-helix are… (intermolecular or intramolecular)

A

intramolecular.

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23
Q

β-sheets are formed when two (or more) different regions of the polypeptide (____ amino acids long) lie side-by-side.

A

usually 3-10.

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24
Q

In β-sheets, hydrogen bonds form between which groups?

A

(C=O) and amino H groups of the backbone.

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25
Q

In β-sheets, the R groups extend…

A

above and below the plane of the sheet.

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26
Q

The strands of a β pleated sheet may be…

A

parallel or antiparallel.

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27
Q

How many beta-strands are necessary to make a β-sheet?

A

two or more.

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28
Q

In β pleated sheet, hydrogen bonds are… (intermolecular or intramolecular)

A

intermolecular.

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29
Q

Tertiary structure is the overall…

A

3D structure of a polypeptide.

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30
Q

Tertiary structure involves interactions between which groups?

A

R groups.

31
Q

Tertiary structure is made up of combinations of…

A

alpha helices and beta pleated sheets.

32
Q

The tertiary structure may be the…

A

final structure.

33
Q

Proteins consisting of only one polypeptide chain have their ___ structure as their final structure.

A

tertiary.

34
Q

Only those proteins that are made of multiple polypeptide chains have a ___ structure.

A

quaternary.

35
Q

Proteins with quaternary structure are known as…

A

oligomeric.

36
Q

Quaternary structures are bonded together through…

A

hydrogen bonds and Van der Waals forces.

37
Q

Hydrogen bonds in quaternary structures exist between different…

A

subunits.

38
Q

Van der Waals forces in quaternary structures exist between…

A

nonpolar side chains.

39
Q

What is meant by “conformational changes” in quaternary protein structure?

A

Change in shape and/or orientation of subunits.

40
Q

Quaternary structure proteins play an important role in…

A

functionality and structure of cellular membranes, mediating transport of ions and macromolecules.

41
Q

Which protein has quaternary structure, made up of 2 alpha subunits and 2 beta subunits?

A

Haemoglobin.

42
Q

Proteins are involved in almost every…

A

biochemical reaction inside biological systems.

43
Q

Actin and myosin are involved in which function of proteins?

A

Mobility.

44
Q

Collagen, Keratin, and elastin are involved in which function of proteins?

A

Structure.

45
Q

Lysozyme and antibodies are involved in which function of proteins?

A

Immunity.

46
Q

Amylases and pepsin are involved in which function of proteins?

A

Enzymes.

47
Q

Insulin and growth hormones are involved in which function of proteins?

A

Hormones.

48
Q

Blood proteins maintain…

A

fluid balance.

49
Q

Haemoglobin and albumin regulate…

A

acid-base.

50
Q

Transferrin and haemoglobin are involved in which function of proteins?

A

Transport.

51
Q

Laminin and nerve growth factors are involved in which function of proteins?

A

Central nervous system.

52
Q

Proteins are also involved in… (in terms of damage)

A

wound healing, regeneration, energy, and satiation.

53
Q

A protein in native conformation is…

A

active and functional.

54
Q

Native conformation occurs due to which type of forces?

A

inter- and intramolecular forces.

55
Q

Denaturation changes protein…

A

shape and causes loss of functionality.

56
Q

Which two factors affect protein shape?

A

temperature and pH.

57
Q

Proteins in living organisms function optimally within…

A

specific conditions.

58
Q

Human proteins require what temperature to maintain native conformation?

A

37°C.

59
Q

Human proteins maintain their native conformation through which forces?

A

electrostatic interactions and hydrogen bonding.

60
Q

Above 37°C, what happens to proteins?

A

Critical inter- and intramolecular forces are disrupted, leading to denaturation.

61
Q

Denaturation leads to loss of…

A

protein function.

62
Q

As temperature increases (below the optimum), what happens to the reaction velocity of a protein?

A

It increases.

63
Q

What happens to the reaction velocity when the temperature rises above the optimum?

A

Denaturation takes place, decreasing velocity.

64
Q

pH levels must be maintained within a ___ in living organisms.

A

narrow range.

65
Q

As pH levels increase or decrease, the environment becomes more…

A

basic or acidic.

66
Q

Changes in pH can cause what to happen to bonds holding proteins together?

A

Break down (leading to denaturation).

67
Q

Denaturation leads to a loss of…

A

protein function.

68
Q

The optimal pH for pepsin (stomach enzyme) is approximately…

A

2.

69
Q

The optimal pH for trypsin (intestinal enzyme) is approximately…

A

8.

70
Q

Therapeutic proteins are genetically engineered versions of…

A

naturally occurring human proteins.

71
Q

Therapeutic proteins with enzymatic activity can…

A

replace a deficient protein, amplify an existing pathway, or have a new functional role.

72
Q

Therapeutic proteins with targeting activity can…

A

interfere with another target molecule or deliver other compounds.

73
Q

Therapeutic proteins can…

A
  • be used as vaccines.
  • interfere with a target molecule,
  • develop immunity to foreign organisms,
  • manage autoimmune diseases,
  • or manage various cancers.
74
Q

How can therapeutic proteins be used in diagnostics?

A

As purified and recombinant compounds.

Biotechnology Mid Term (9 decks)

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