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Grade 12 Bio > Unit 1- > Flashcards

Unit 1- Flashcards

1
Q

-OH

A

Hydroxyl

Polar so soluble in h2o

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2
Q

Where are hydroxyls found?

A

Sugars and alcohols

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3
Q

-COOH

A

Carboxyl

Polar so soluble in H2O

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4
Q

What does a carboxyl do to a molecule?

A

Makes it acidic

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5
Q

-CO

A

Carbonyl

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6
Q

Where is a carbonyl found?

A

On aldehydes and ketones

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7
Q

-NH2

A

Amino

Found on amino acids

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8
Q

What’s does an amino do to a molecule?

A

Makes the solution basic

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9
Q

PO4 2-

A

Phosphate

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10
Q

Where are phosphates found?

A

Found on nucleotides and nucleic acids.

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11
Q

What do phosphates help with?

A

Energy transfer

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12
Q

-SH

A

Sulfhydryl

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13
Q

Where are sulfylhydryls found?

A

Found in cellular molecules

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14
Q

Triose

A

Sugar with 3 carbon atoms. C3H6O3

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15
Q

Pentose

A

Sugar with 5 carbon atoms. C5H10O5

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16
Q

Hexoses

A

Sugar with 6 carbon atoms C6H12O6

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17
Q

Aldoses

A

Carbonyl located on the last carbon in the chain

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18
Q

Ketoses

A

Carbonyl located on a carbon in the middle of the chain

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19
Q

4 types of macromolecules

A

Carb protien lipid nucleic acid

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20
Q

Monomer of carbs

A

Monosaccharides

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21
Q

Monomer of lipids

A

Glycerol and fatty acids

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22
Q

Monomer of protien

A

Amino acids

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23
Q

Monomer of nucleic acid

A

Nucleotides

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24
Q

What happens when pentoses and hexoses enter water

A

They turn from linear to cyclic

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25
Q

Starch

A

(Poly) formed in chloroplasts

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26
Q

Form of starch

A

20% straight amylose

80% branches amylopectin

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27
Q

Glycogen

A

(Poly) more branched than amylopectin. Energy storage molecule found in liver and muscle cells. Hydrolysis to glucose during physical exercise

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28
Q

Cellulose

A

Straight chain found in cell wall. Humans can’t digest it

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29
Q

Chitin

A

Found in cell wall of fungi and exoskeleton of insects and crustaceans

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30
Q

Function of lipids

A

Store energy. Build membrane and other cell parts. Chemical signals (hormones)

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31
Q

Families of lipids

A

Fat wax steroid phospholipid

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32
Q

Energy in 1 g of fat and carbs

A 
Fat = 38kj
Carbs = 17 kj
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33
Q

Fats are stored in animals by

A

Droplets in cell of fat tissue. Thermal insulation in penguins.

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34
Q

Fats are stored in plants by

A

Stored in seeds as oil

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35
Q

Saturated fat

A

Single bonds between carbon atoms

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36
Q

Unsaturated fat

A

One or more double bonds between c atoms

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37
Q

Animal fat

A

Saturated molecules fit tight together so solid at room temp.

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38
Q

Plant oil

A

Polyunsaturated so bends in molecules make them not fit together. So liquid at room temp

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39
Q

Difference between glucose and galactose

A

The oh on carbon 4 is down on glucose. The oh on carbon 4 is up on galactose.

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40
Q

Steroid example

A

Cholesterol. Testosterone. Estrogen.

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41
Q

Primary protein structure

A

Unique sequence of amino acids in the polypeptide chain. Under the control of DNA

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42
Q

What is a residue

A

Each amino acid in the polypeptide chain

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43
Q

Secondary protein structure 2 types

A

Alpha helix and beta pleated sheets

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44
Q

Alpha helix

A

Hydrogen bonds form between the O of a carboxyl group and the H of a different amino. Repeated H bonds shape the polypeptide into a coil.

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45
Q

Alpha helix example

A

Alpha keratin

Found in hair

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46
Q

Beta pleated sheets

A

When 2 polypeptide chains lie parallel to each other and Hydrogen bonds form between the carboxyl and adjacent amino strand

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47
Q

Beta pleated sheet example

A

In spider silk and can stretch 40 % before breaking while steal will only bend 8%

48
Q

Tertiary structure

A

The protein folds because various points on the structure are attracted to eachother. Strongest bonds are disulfide bridges. There are also weak ionic bonds and hydrophobic bonds.

49
Q

Quaternary structure

A

When 2 or more amino acid chains link together to make a more complex protien.

50
Q

Conjugated protien

A

Protien containing non protien material.

51
Q

Prostetic group

A

The non protien part in a conjugated protein

52
Q

Waxes

A

Long fatty acids liked to alcohols or carbon rings. Pliable and hydrophobic so then waterproof

53
Q

Example of waxes 3

A

Cutin- epidermal cell of plants to conserve h2o
Birds- wax keeps feathers dry
Bees-beeswax used for honeycomb

54
Q

Functions of proteins 4

A

Enzymes-catalysts
Immunoglobulins-protect against pathogens
Transport-hemoglobin or phloem
Structure-keratin collagen fibrin

55
Q

When dissolved in water what happens to some proteins

A

They become amphipratic which is acidic and basic zwitter ions

56
Q

3 types of amino acids

A

Polar non polar and charged

57
Q

Polar amino acid

A

Hydrophilic. Side chains contain oxygen which makes them very electronegative

58
Q

Non polar amino acid

A

Hydrophobic side chains are mostly carbon and hydrogen

59
Q

Charge amino acid

A

Acidic or basic. Side chains have carboxyl or amino groups

60
Q

What is the 3D shape of a protien known as and what is it determined by

A

Confirmation

Sequence of amino acids

61
Q

Polypeptide

A

Multiple amino acids linked together

62
Q

What are amino acids held together by

A

Peptide bonds

63
Q

Structural protien

A

Framework ex hair

64
Q

Defensive protien

A

Infection fighters. Ex. Antibodies

65
Q

Signal proteins

A

Messenger. Ex hormones

66
Q

Carrier proteins

A

Transport all materials. Ex hemoglobin

67
Q

Recognition/ receptor

A

Cell markers. Ex. Major histocomparibility complex

68
Q

Enzyme protien

A

Catalyst ex amylase

69
Q

Motile protien

A

Movement ex actin and myosin

70
Q

Transcription to amino acids order

A

DNA transcribed to mRNA. mRNA translated to protien at ribosomes. During translation amino acids are linked by peptide bonds

71
Q

A terminus

A

Free amino group at end of polypeptide

72
Q

C terminus

A

Free carboxyl at end of polypeptide

73
Q

How many essential amino acids are there

A

9 that must be ingested for survival. But there are 20 total but the rest are made by the body

74
Q

Plasmodesmata

A

In plants. Tiny cell receptors that act like bridges of cytoplasm that pass through adjacent cell walls and link them allowing rapid exchange of materials

75
Q

Belt desmosomes

A

Line body cavities Ike the mouth and form protective layers like the skin

76
Q

Spot desmosomes

A

Hold cells together and anchor the intermediate filaments of the cytoskeleton. Found in cells of tissues that have a lot of wear and tear like outer layers of skin

77
Q

Hemidesmosome

A

Attaches a cell to extra cellular matrix

78
Q

How does communication occur thru cells?

A

Gap junctions. They are protien lined pores that connect adjacent cells

79
Q

Integral membrane proteins

A

Anchored in place. Projecting regions must have polar R groups. Allows different things to move through

80
Q

Integral protien that allows water to travel through it

81
Q

Hydroxyl + hydroxyl

82
Q

Hydroxyl + carboxyl

83
Q

Carboxyl + carboxyl

84
Q

2 phosphoric acids

A

Phosphate annhydride

85
Q

Hydroxyl + phosphoric acid

A

Phosphate ester

86
Q

How to develop a protien

A

Add them together int he order they’re given and the number of bonds is he number of waters produced

87
Q

Protein denaturation

A

Results in change of 3 D shape of a protein. Loses its function

88
Q

Causes of denaturation

A

Temperature ph ionic concentration and heavy metal salts

89
Q

If the denaturing agent is removed it may

A

Return to normal or remain denatured because the damage was too much

90
Q

Dangerous denaturation examples

A

Fever causes denaturation of brain causing seizure and coma

91
Q

Helpful denaturation examples

A

Hair styling chemicals and heat used to curl or straighten hair

92
Q

Competitive inhibition

A

Enters active site and blocks substrate from binding. Can be reversed by increased substrate concentration

93
Q

Non competitive inhibition

A

Attaches to enzyme but not at active site. Causes change of shape and loses affinity. Or affects part of enzyme that’s active in catalysis. Non reversible.

94
Q

Gibbs free energy equals

A

G reactants -G products

95
Q

Lose electrons

96
Q

Gain electrons

97
Q

Negative G

A

Exergonic so catabolic

98
Q

Positive G

A

Endergonic so anabolic

99
Q

Glycoproteins

A

I’m phospholipid bilayer. Proteins attach carb chains. Help with cellular recognition and immune response. Receptors for hormones

100
Q

Glycoproteins and glycolipids

A

Together they stabilize the phospholipid bylayer

101
Q

Cholesterol in fluid mosaic model

A

Lipid. Regulates membrane fluidity

102
Q

Glycolipids

A

Surface receptors

103
Q

Integral protien in bilayer

A

Control entry and removal of molecule from the cell

104
Q

Induced fit model

A

Functional group on substrate comes close to functional group on amino acids at active site. Close interaction causes protien to change shape to better accommodate the substrate

105
Q

Active site

A

Binds to substrate

106
Q

Allosteric site

A

Binds a substance that may stimulate or inhibit the enzymes activity

107
Q

Activator inhibitor

A

Binds to allosteric site and stabilizes active form of enzyme. Available to bind with substrate

108
Q

Allosteric inhibitor

A

Binds to allosteric site. Stabilizes inactive form of enzyme. Active site will be unable to bind with substrate when enzyme is in inactive form

109
Q

Feedback inhibition

A

Method of metabolic control. Product formed later in a sequence of reactions allosterically inhibits an enzyme that catalyzes a reaction earlier in the process. Happens when there’s too much. So the body gives negative feedback and regulates itself.

110
Q

Types of integral proteins 6

A

Hormone receptor, enzymes, electron carriers, passive transport, active transport pumps and attachment to cytoskeleton

111
Q

Globular protein

A

Hemoglobin

112
Q

Hyponatrimia

A

When there is excess body fluid in the body so it enters the cells and they expand too much. Dilutes Na+ serum.

113
Q

When you have hyponatrimia

A

Less than 135 concentration of sodium ions in serum

114
Q

Types of bonds in tertiary structures strong to weak

A

Disulfide bridge, h bonds, ionic bonds, hydrophobic bonds

115
Q

Anabolic

A

Making of molecules

116
Q

Catabolic

A

Breaking down of molecules

Grade 12 Bio (3 decks)

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