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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
A singular molecule making up the end of a wax molecule (i.e. Stearic Acid)
Fatty Acid
26
The hydrophilic end of a wax molecule that uses any other alcohol than glycerol (i.e. Oleic Alcohol)
Alcohol
27
oldest of all the biological compounds
Terpenes
28
They are also the most diverse biological molecules
Terpenes
29
These molecules are best known as the scent molecules of plants, as they are abundant in essential oils used in cosmetics
Terpenes
30
In food products, they are important nutritive compounds (i.e. vitamins)
Terpenes
31
They are also the ones that trigger the "addiction" of humans in Cannabis sativa
Terpenes
32
lipids that are similar in structure to fats and oils
Phospholipids
33
How many fatty acids are present in the tail of phospholipid?
2
34
What is present in the head of a phospholipid structure?
Phosphate group
35
They are the building blocks of the cell membranes
Phospholipids
36
molecules crucial to animals and are the building blocks of the sex hormones
Steroids
37
chemical messengers produced in one part of the body, they travel to and cause changes in another part of the body.
Hormones
38
What elements is protein comprised of?
Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur
39
It accounts for half of the dry weight of most cells
Protein
40
These biomolecules are also the most complex in structure
Protein
41
They are the most versatile of all the biomolecules, as they are crucial element in almost everything that happens within the cell
Protein
42
They also function in the regulation of chemical reactions in the body (enzymes), as they may accelerate or stall reactions
Proteins
43
What are the building blocks of proteins?
Amino Acids
44
How many amino acids are in the human body?
20
45
Classifications of Amino acids according to their functional groups
Polar, Non-Polar, and electrically charged amino acids
46
Classifications of Amino acids according to whether the body can produce them or not
Essential and Non-essential amino acids
47
Amino acids used for the maintenance of the nervous system
Asparagine
48
Amino acid used for body alertness, collagen and keratin synthesis, and skin tensile strength maintenance
Cysteine
49
Amino acid that serves as stress protein and immune booster
Glutamine
50
Amino acid that serves as 'food source' of the brain
Serine
51
Amino acid that serves as 'fight-or-flight' response protein, precursor of adrenaline and dopamine
Tyrosine
52
Example of polar essential amino acid
Threonine
53
Example of Non-Polar Essential Amino Acid
Leucine, Isoleucine, Valine, Methionine, Phenylalanine, Tryptophan
54
Example of Electrically Charged Essential Amino Acid
Histidine and Lysine
55
Example of Polar Non-Essential Amino Acids
Asparagine, Cysteine, Glutamine, Serine, Tyrosine
56
Example of Non-Polar Non-Essential Amino Acids
Alanine, Glycine, Proline
57
Amino acid that controls glucose during glycolysis
Alanine
58
Amino acid used for neurotransmittance control
Glycine
59
Amino acid used for muscle and joint maintenance
Proline
60
Amino acid used for blood pressure maintenance
Arginine
61
Amino acid used for energy maintenance and fatigue reduction
Aspartic Acid
62
Amino acid used for nervous system overall maintenance
Glutamic Acid
63
The structure of a protein is defined by its __
Conformation
64
arrangement of the amino acids in the protein megastructure
Conformation
65
Levels of Protein Structure
Primary, Secondary, Tertiary, Quaternary Structure
66
Simplest level of protein structure
Primary Structure
67
It is simply the arrangement of amino acids in a chain
Primary Structure
68
Protein structure that is dependent on the interactions of the functional groups
Secondary Structure
69
2 classifications of secondary structure in protein
α-helix and β-pleated sheet
70
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
α-helix
71
segments of the chain line up side by side and become linked via hydrogen bonds, forming a sheet
β-pleated sheet
72
Protein structure that is dependent on the interactions of the R-group in the amino acids
Tertiary Structure
73
Forms the 3D structure of the protein, and is oftentimes the final folded structure of proteins
Tertiary Structure
74
It is common in proteins whose primary structure is made up of multiple chains
Quaternary Structure
75
Allows chemical reactions to occur in living things
Enzymes
76
protect the body from infection
Antibodies
77
energy required to start a chemical reaction
activation energy
78
proteins which reduce activation energy allowing chemical reactions to occur in living things.
Enzymes
79
inorganic/organic molecules that speed up chemical reactions
Catalysts
80
it is where the chemical reaction occurs.
active site
81
the molecule that the enzyme acts on.
substrate
82
The fact that the active site can only accept one type of substrate is known as ___
Enzyme specificity
83
Two ideas about enzyme action
Lock and Key model and Induced Fit model
84
In this model, the enzyme puts stress on the bond which reduces the amount of energy needed to break apart the substrate
Lock and key model
85
In this model, the substrate causes (induces) the enzyme to change shape which allows the substrate to fit into the active site
Induced Fit Model
86
Factors that affect enzyme activities
Environmental conditions, cofactors and coenzymes, and enzyme inihibitors
87
two types of inhibition
competitive and non-competitive inhibition
88
If a protein loses its shape, it loses its function, a protein that loses its shape is said to be ___
Denatured
89
What happens when an enzyme is denatured?
Substrate can't enter the active site
90
Enzyme in the mouth that breaks down starches into disaccharides
Salivary Amylase
91
Enzyme in the stomach that breaks down proteins into large peptides
Pepsin
92
Enzyme in the small intestines (from pancreas) that continues the breakdown of starch
Amylase
93
Enzyme that continues the breakdown of protein
Trypsin
94
Enzyme that breaks down fats
Lipase
95
Enzyme in the small intestine that breaks down remaining disaccharides into monosaccharides
Maltase, Sucrase, Lactase
96
Enzyme that breaks down dipeptides into amino acids
Peptidase

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