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SBI 3UI > Unit 1 > Flashcards

Unit 1 Flashcards

1
Q

Cellular respiration

A

The chemical reactions needed to break down carbs and other molecules to transfer chemical energy to ATP

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2
Q

Cellular respiration equation

A

C6H12O6 + 6O2 –> 6H2O + 6CO2 + Energy

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3
Q

Hydrogen bonding

A

Weak bonds between molecules where a hydrogen atom is present

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4
Q

4 properties of water which make life possible as we know it

A

Remains liquid over a wide temp range
Dissolves most substances
Changes temperature gradually
Only pure substance to expand when frozen which allows ice to float

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5
Q

Disaccharide

A

A double sugar is made of 2 simple sugars bonded together

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6
Q

What makes something a condensation reaction?

A

When h2o is present

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7
Q

The opposite of condensation reaction is

A

Enzymatic hydrolysis. Which is digestion

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8
Q

Glucose + glucose

A

Maltose + water

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9
Q

Glucose + fructose

A

Sucrose+ water

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10
Q

Glucose + galactose

A

Lactose + water

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11
Q

Polysaccharides

A

A complex carb consisting of many simple sugars linked together

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12
Q

Organic compound

A

A compound that contains both carbon and hydrogen They form a permanent part of living cells and have a carbon backbone

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13
Q

Hypotonic in animal cell

A

Lysis cell death

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14
Q

Hypertonic in plant cell

A

PlassmolyZed

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15
Q

Hypertonic in animal cell

A

Crenation. Shrivelled

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16
Q

Osmosis

A

Movement of water through a semipermeable membrane from high concentration to low concentration. Occurs in blood and blood cells

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17
Q

Diffusion.

A

Movement of a substance from and area of high concentration to low concentration. Affected by temperature and concentration. Ex. Tea and hot water

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18
Q

Phagocytosis

A

Large solid particles are engulfed by a cell. Turns into a vacuole or vesicles. Atp required

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19
Q

Pinocytosis

A

Occurs when particles to be taken into cells are in liquid droplets. Food vacuole forms at the end. Atp required

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20
Q

Phospholipid

A

Triglycerides with only 2 fatty acids bonded to a glycerol. The third glycerol rxn site is bonded to a nitrogen containing molecule

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21
Q

Hydropholic region of phospholipid

A

The head of the phospholipid is polar therefore dissolves in water

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22
Q

Hydrophobic region of phospholipid

A

The tail of the phospholipid is made of 2 fatty acids. The hydrocarbon chains are non polar and afraid of water

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23
Q

Ampiphilic compound

A

A compound molecule with areas of both polar and nonpolar regions

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24
Q

Cholesterol in the cell membrane

A

Only in animal cells. It prevents cell death when it is exposed to extreme temperatures. Keeps it rigid and flexible and functional.

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25
Q

What kind of lipid is cholesterol

A

Steroid

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26
Q

Integral protiens

A

Moves things in and out of the cell. In cell membrane

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27
Q

Glycoproteins

A

Marks you as you. So they are different in everyone

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28
Q

Peripheral protiens

A

Receptors for enzymes and protiens

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29
Q

What H:O ratio is in carbs

A

2:1

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30
Q

Carbs produce what type of energy

A

Provide short or long term energy

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31
Q

Important types of hexoses

A

Glucose. Galactose.

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32
Q

Important types of pentoses

A

Ribose and deoxyribose

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33
Q

Starches

A

E storage molecules in plants. Result of the coiling of glucose units

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34
Q

Glycogen

A

E storage in animals. Has a lot of branches coming off it

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35
Q

Cellulose

A

Humans can’t digest it. Major cell wall component. Forms microtubules with H bonds between them so they don’t spiral

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36
Q

Lipids are Hydropholic or phobic?

A

Hydrophobic

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37
Q

Are lipids long or short term energy storage

A

Long term energy

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38
Q

Good things about fats

A

Cushion organs. Insulation to conserve energy.

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39
Q

How much more energy does lipids have then fats

A

2.25 times more energy per gram

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40
Q

What is each fat molecule composed of

A

3 fatty acids and 3 carbon molecs called glycerol

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41
Q

Why is it called a triglyceride

A

Bc there is 3 fatty acids

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42
Q

Saturated fat

A

Each carbon is bonded to 4 atoms. Bad fats. Will be solid at room temperature

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43
Q

Unsaturated fat

A

Double bonds exist writhing fatty acids. Liquid at room temperature

44
Q

Monounsaturated

A

1 double bond

45
Q

Polyunsaturated

A

Several double bonds

46
Q

Types of bonds in tryglicerides

A

Ester bonds

47
Q

Where are protiens structurally used

A

In bones muscles, ligaments and tendons

48
Q

Enzymes

A

Speed up chemical reactions. They transport molecules in and out of the cell

49
Q

Hormones are

A

Chemical messengers in the body

50
Q

Protiens are made up of things called

A

Amino acids

51
Q

Each amino acid has a central carbon with

A

An h atom. An amino group h2n and a carboxylate group (cool). And an R which is different for each acid

52
Q

Amino acid + amino acid

A

Dipeptide

53
Q

Polypeptide

A

When many dipeptides are bonded together

54
Q

Bonds in protien structures

A

Peptide bonds. Why it’s called a Dipeptide

55
Q

What happens if a protien is exposed to any extremes

A

It become denatured. Loses its shape and is useless

56
Q

If the R group on the protien is polar

A

Then the acid is soluble

57
Q

If the R group on the protien is nonpolar

A

The acid is insoluble

58
Q

How many amino acids does your body need

A

20 amino acids

59
Q

How many amino acids does your body make

A
  1. So 9 need to be in the dirt
60
Q

Primary level protein structure

A

The exact linear sequence of amino acids in the protien

61
Q

Secondary level protien structure

A

Each amino acid reacts with its neighbour. There is hydrogen bonding between all acids but far apart

62
Q

Types of shapes in secondary level protiens

A

Alpha helix - pig tail

Beta pleated sheet - accordion

63
Q

Tertiary level protien structure

A

Depends strongly on secondary structure. Makes the shape 3 D

64
Q

In the tertiary level when it’s made of beta pleated sheets it makes

A

Fibers that have a structural function

65
Q

In tertiary levels when it’s made of alpha Helixs they form

A

Globular sheets which are sensitive and if a single amino acid changes it loses its function.

66
Q

Type of bond in tertiary level proteins

A

Disulfide bridges

67
Q

Quaternary level of protien structure

A

When 2 or more polypeptide chains link together. Also makes air pockets. Ex. Hemoglobin

68
Q

Conjugated protien

A

Protein with something attached to it

69
Q

Globular protiens

A

Soluble in aqueous solutions and diffuse readily. They move things And have a spherical shape. Ex. Hemoglobin

70
Q

Fibrous proteins

A

Water insoluble and physically tough. Structural protectors. The polypeptide chains are parallel and strong

71
Q

Structural protien example

A

Keratin in hair and nails. And collagen

72
Q

Transport protien example

A

Hemoglobin

73
Q

Protective protien example

A

Antibodies in the blood

74
Q

Membrane protiens

A

Play active role in diffusion but still passive transport

75
Q

Carrier protiens in membrane

A

Specific shape and only accept non charged molecules with the same exact shape. Movement occurs both in and out of cell

76
Q

Channel protiens

A

Tunnel shaped allow ions in to pass through membrane. The channel and protien are oppositely charged

77
Q

Function of cell membrane protiens

A

Transport channels, receptor sites for enzymes, cell identity markers, attachment of cytoskeleton, cell adhesion and insulin receptor site on outside while metabolic rxn inside

78
Q

DNA pairs

A

Adenine and thymine

Cytosine and guanine

79
Q

RNA pairs

A

Adenine and uracil

Cytosine and guanine

80
Q

Structure of Dna

A

Double helix. Hydrogen bonds hold them together. It’s 2 strands

81
Q

Nucleic acids

A

Direct the growth and development in living organisms by chemical code

82
Q

DNA contains instructions for

A

RNA

83
Q

RNA has instructions to make

A

Protiens

84
Q

Protiens make the

A

Structure of the cell and the protien

85
Q

Structure of nucleus acids and 3 components

A

Long chains called nucleotides. Made of pentode sugar. Phosphate and n containing base

86
Q

4 stages of cellular respiration

A

Glycolysis, transition reaction, krebs cycle, electron transfer chain (etc)

87
Q

Glycolosis

A

Occurs in cytoplasm. Does not use O2. Glucose molecules snaps in 2. 2 atp produced

88
Q

Transition reaction

A

Connects glycolysis to Krebs cycle. 2 carbon molecules emerged the mitochondria. Co2 produced and released

89
Q

Krebs cycle

A

Occurs in matrix. Releases co2. Makes atp. Cycle turns 2 times for each glucose molec so a total of 4 co2 are produced and 2 atp

90
Q

Electron transfer chain ETC

A

The movement of electrons down the chain the electrons are full of energy from the breakdown. H2 o is formed. Aerobic reaction. Occurs on the cristae with the enzymes. 32 atp are produced in eukaryotes.

91
Q

In ATP when the bonds break how much energy is released

A

12000 on the first 12000 on the second and 3000 on the third. The first bond is relatively unstable and easy to break

92
Q

What happens in the matrix of the mitochondria

A

Krebs cycle

93
Q

What happens in the cristae of the mitochondria

A

Where most of ATP is produced in electron transfer chain

94
Q

Bonds in disaccharides (carbs)

A

Glycosidic bonds

95
Q

Bond in maltose

A

Alpha 1-4 glycosidic bond

96
Q

Bonds in protiens

A

Peptide bonds. Why they are called dipeptides

97
Q

What happens in the grana?

A

Where energy is produced in chloroplasts using light

98
Q

What is the grana made of?

A

Thylakoids

99
Q

What happens in the stroma of the chloroplast

A

Where energy reactions occur with no light

100
Q

Bonds in triglycerides

A

Ester bonds

101
Q

How do DNA and RNA differ?

A

Different nitrogenous bases

102
Q

How does the pentose sugar differ in Dna and rna?

A

Deoxyribose and ribose

103
Q

How many polynucleotide strands are in DnA and RNA

A

DNA 2 strands. RNA 1 strand

104
Q

Where is DNA located

A

Nucleus mitochondria and cytoplasm

105
Q

Where is RNA located

A

Nucleus and cytoplasm

SBI 3UI (6 decks)

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