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Modern Biology > L3 - Lipids and Proteins > Flashcards

L3 - Lipids and Proteins Flashcards

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1
Q

biomolecules that are considered as hydrophobic or water-hating

A

Lipids

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2
Q

they do not exhibit polymerization, but are large molecules in their own respect

A

Lipids

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3
Q

Lipids can be classified as?

A

Simple and Complex Lipids

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4
Q

What does simple lipids include?

A

Fats/Oils, Waxes, Terpeenes

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5
Q

What does complex lipids include

A

Phospholipids and steroids

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6
Q

lipids that serve as the storage units of energy

A

Fats/Oils

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7
Q

Difference between fats and oils?

A

Fats came from animals while oils came from plants

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8
Q

Double bonds are absent; tight packing of molecules happen

A

Saturated Fat/Oil

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9
Q

Double bonds are present; tight packing of molecules is impossible due to contortions caused by the bonds

A

Unsaturated Fat/Oil

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10
Q

Example of Saturated Fats

A

meat, butter, dairy products

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11
Q

Example of Unsaturated Fats

A

vegetable oils

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12
Q

These fats increase levels of ‘bad’ cholesterol (low-density lipoprotein), which clogs arteries

A

Saturated Fats

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13
Q

These fats increase levels of ‘good’ cholesterol (high-density lipoprotein), escorts the LDL into the liver where it is removed from the body

A

Unsaturated Fats

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14
Q

An alcohol unique to fats and is rich in hydroxyl, making it hydrophilic

A

Glycerol

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15
Q

End of a ‘fat’ molecule that readily dissolves in water

A

Hydrophilic Head

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16
Q

Links that form when the carboxyls of the fatty acids react with the hydroxyls of Glycerol during bonding

A

Ester linkages

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17
Q

Triad of molecules that are inherently hydrophobic, and make up the tail of the fat molecule

A

Fatty Acids

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18
Q

The end of a fat molecule rich in methyls, which do not readily dissolve in water

A

Hydrophobic Tail

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19
Q

lipids that is formed between a long alcohol chain and a fatty acid molecule through ester synthesis

A

Waxes

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20
Q

Formation of an ester through dehydration synthesis between a hydroxyl and a carboxyl

A

Ester Synthesis

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21
Q

They are found as coatings of plants and animals, as well as part of the blubber of animals

A

Waxes

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22
Q

They function as a preventive barrier against water loss

A

Waxes

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23
Q

Found on the surface of leaves and found on animal hair to keep it pliable

A

Waxes

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24
Q

Found on the feathers of water birds to prevent them from becoming waterlogged

A

Waxes

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25
Q

A singular molecule making up the end of a wax molecule (i.e. Stearic Acid)

A

Fatty Acid

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26
Q

The hydrophilic end of a wax molecule that uses any other alcohol than glycerol (i.e. Oleic Alcohol)

A

Alcohol

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27
Q

oldest of all the biological compounds

A

Terpenes

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28
Q

They are also the most diverse biological molecules

A

Terpenes

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29
Q

These molecules are best known as the scent molecules of plants, as they are abundant in essential oils used in cosmetics

A

Terpenes

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30
Q

In food products, they are important nutritive compounds (i.e. vitamins)

A

Terpenes

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31
Q

They are also the ones that trigger the “addiction” of humans in Cannabis sativa

A

Terpenes

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32
Q

lipids that are similar in structure to fats and oils

A

Phospholipids

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33
Q

How many fatty acids are present in the tail of phospholipid?

A

2

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34
Q

What is present in the head of a phospholipid structure?

A

Phosphate group

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35
Q

They are the building blocks of the cell membranes

A

Phospholipids

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36
Q

molecules crucial to animals and are the building blocks of the sex hormones

A

Steroids

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37
Q

chemical messengers produced in one part of the body, they travel to and cause changes in another part of the body.

A

Hormones

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38
Q

What elements is protein comprised of?

A

Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur

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39
Q

It accounts for half of the dry weight of most cells

A

Protein

40
Q

These biomolecules are also the most complex in structure

A

Protein

41
Q

They are the most versatile of all the biomolecules, as they are crucial element in almost everything that happens within the cell

A

Protein

42
Q

They also function in the regulation of chemical reactions in the body (enzymes), as they may accelerate or stall reactions

A

Proteins

43
Q

What are the building blocks of proteins?

A

Amino Acids

44
Q

How many amino acids are in the human body?

A

20

45
Q

Classifications of Amino acids according to their functional groups

A

Polar, Non-Polar, and electrically charged amino acids

46
Q

Classifications of Amino acids according to whether the body can produce them or not

A

Essential and Non-essential amino acids

47
Q

Amino acids used for the maintenance of the nervous system

A

Asparagine

48
Q

Amino acid used for body alertness, collagen and keratin synthesis, and skin tensile strength maintenance

A

Cysteine

49
Q

Amino acid that serves as stress protein and immune booster

A

Glutamine

50
Q

Amino acid that serves as ‘food source’ of the brain

A

Serine

51
Q

Amino acid that serves as ‘fight-or-flight’ response protein, precursor of adrenaline and dopamine

A

Tyrosine

52
Q

Example of polar essential amino acid

A

Threonine

53
Q

Example of Non-Polar Essential Amino Acid

A

Leucine, Isoleucine, Valine, Methionine, Phenylalanine, Tryptophan

54
Q

Example of Electrically Charged Essential Amino Acid

A

Histidine and Lysine

55
Q

Example of Polar Non-Essential Amino Acids

A

Asparagine, Cysteine, Glutamine, Serine, Tyrosine

56
Q

Example of Non-Polar Non-Essential Amino Acids

A

Alanine, Glycine, Proline

57
Q

Amino acid that controls glucose during glycolysis

A

Alanine

58
Q

Amino acid used for neurotransmittance control

A

Glycine

59
Q

Amino acid used for muscle and joint maintenance

A

Proline

60
Q

Amino acid used for blood pressure maintenance

A

Arginine

61
Q

Amino acid used for energy maintenance and fatigue reduction

A

Aspartic Acid

62
Q

Amino acid used for nervous system overall maintenance

A

Glutamic Acid

63
Q

The structure of a protein is defined by its __

A

Conformation

64
Q

arrangement of the amino acids in the protein megastructure

A

Conformation

65
Q

Levels of Protein Structure

A

Primary, Secondary, Tertiary, Quaternary Structure

66
Q

Simplest level of protein structure

A

Primary Structure

67
Q

It is simply the arrangement of amino acids in a chain

A

Primary Structure

68
Q

Protein structure that is dependent on the interactions of the functional groups

A

Secondary Structure

69
Q

2 classifications of secondary structure in protein

A

α-helix and β-pleated sheet

70
Q

Secondary structure where the carbonyl of one amino acid becomes linked to the amino group of another amino acid 4 units down the chain, forming a helical shape

A

α-helix

71
Q

segments of the chain line up side by side and become linked via hydrogen bonds, forming a sheet

A

β-pleated sheet

72
Q

Protein structure that is dependent on the interactions of the R-group in the amino acids

A

Tertiary Structure

73
Q

Forms the 3D structure of the protein, and is oftentimes the final folded structure of proteins

A

Tertiary Structure

74
Q

It is common in proteins whose primary structure is made up of multiple chains

A

Quaternary Structure

75
Q

Allows chemical reactions to occur in living things

A

Enzymes

76
Q

protect the body from infection

A

Antibodies

77
Q

energy required to start a chemical reaction

A

activation energy

78
Q

proteins which reduce activation energy allowing chemical reactions to occur in living things.

A

Enzymes

79
Q

inorganic/organic molecules that speed up chemical reactions

A

Catalysts

80
Q

it is where the chemical reaction occurs.

A

active site

81
Q

the molecule that the enzyme acts on.

A

substrate

82
Q

The fact that the active site can only accept one type of substrate is known as ___

A

Enzyme specificity

83
Q

Two ideas about enzyme action

A

Lock and Key model and Induced Fit model

84
Q

In this model, the enzyme puts stress on the bond which reduces the amount of energy needed to break apart the substrate

A

Lock and key model

85
Q

In this model, the substrate causes (induces) the enzyme to change shape which allows the substrate to fit into the active site

A

Induced Fit Model

86
Q

Factors that affect enzyme activities

A

Environmental conditions, cofactors and coenzymes, and enzyme inihibitors

87
Q

two types of inhibition

A

competitive and non-competitive inhibition

88
Q

If a protein loses its shape, it loses its function, a protein that loses its shape is said to be ___

A

Denatured

89
Q

What happens when an enzyme is denatured?

A

Substrate can’t enter the active site

90
Q

Enzyme in the mouth that breaks down starches into disaccharides

A

Salivary Amylase

91
Q

Enzyme in the stomach that breaks down proteins into large peptides

A

Pepsin

92
Q

Enzyme in the small intestines (from pancreas) that continues the breakdown of starch

A

Amylase

93
Q

Enzyme that continues the breakdown of protein

A

Trypsin

94
Q

Enzyme that breaks down fats

A

Lipase

95
Q

Enzyme in the small intestine that breaks down remaining disaccharides into monosaccharides

A

Maltase, Sucrase, Lactase

96
Q

Enzyme that breaks down dipeptides into amino acids

A

Peptidase

Modern Biology (10 decks)

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