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Bio: Grade 12 > Unit 1 > Flashcards

Unit 1 Flashcards

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Biology 101 flashcards
1
Q

organic chemistry:

A

organic molecules formed by a carbon frame

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2
Q

catenation:

A

the ability for carbon to make chains w itself

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3
Q

hydro carbons

A

organic molecules that are formed when carbon is bonded to hydrogen alone

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4
Q

condensation reaction:

A

atoms are removed when 2 small molecules join to make 1 big molecule

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5
Q

condensation reactions are how ________ _____ _____ are made

A

synthetic natural polymers are preformed

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6
Q

dehydration reaction:

A

form of condensation where the removed molecule (to connect the 2 smaller ones) is water.

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7
Q

hydrolysis reaction:

A

(opposite reaction). the cutting (or lysing) of a large molecule into smaller molecules using water.

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8
Q

hydrolysis is…

A

an important process in living systems as our body used this process to break down proteins, fats, carbs, nucleic acids and more

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9
Q

redox reaction aka _____:

A

oxidation-reduction

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10
Q

oxidation:

A

when an atom or molecule loses electrons

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11
Q

reduction:

A

when an atom or molecule gains electrons

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12
Q

in living systems, redox reactions…

A

involve the transfer of free energy from one molecule to another

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13
Q

a simpler way to identify a redox reaction is when…

A

a hydrogen or oxygen atom is gained or lost

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14
Q

reduction (in perspective of oxygen and hydrogen) is when…

A

oxygen is lost
or
hydrogen is gained

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15
Q

oxidization (in perspective of Oxygen and hydrogen) is when…

A

Oxygen is gained
or
Hydrogen is lost

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16
Q

carbohydrate:

A

provides body with energy

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17
Q

monosaccharide:

A

(simple sugars) simplest form of a carb that contains 1 ring

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18
Q

ex of monosaccharide glucose:

A
  • can be shown in a linear chain or ring structure

- carries in the blood and transported to the cells to make cellular energy-

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19
Q

various types of sugar include:

A

galactose, xylose, fructose + more. (they have similar structures but different arrangement of atoms

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20
Q

how many carbon structures make up a DNA structure:

A

5 carbon structures make up the dna structure. such as monosaccharides, ribose, and deoxyribose

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21
Q

disaccharides:

A

combination of 2 monosaccharides (through a dehydration/ hydrolysis reaction) to form a disaccharide. (2 rings)

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22
Q

ex: table sugar (sucrose) is a disaccharide of:

A

glucose and fructose joined by a hydrolysis reaction

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23
Q

disaccharide linkages are called:

A

glycosidic linkages

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24
Q

polysaccharides:

A

(large molecules w 3 or more rings) these carbohydrates are polymers made up of many monosaccharides joined together.

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25
Q

polysaccharides are thousands…

A

of sugars in linear or branched structures. (includes molecules such as cellulose (wood) and starch which is found in rice and pasta).

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26
Q

starch in chloroplast is componentized as:

A

aylose and amylopectin

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27
Q

aylose:

A

straight chain

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28
Q

amylopectin:

A

branches & coils (insoluble in water)

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29
Q

cellulose:

A

polysaccharide in plants that can’t be broken down by humans

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30
Q

glycogen:

A

energy storage in heterotrophs like amylopectin but more branches stores in liver and muscles

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31
Q

fats/lipids:

A

carbon, hydrogen, oxygen

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32
Q

hydrophobic:

A

molecules that don’t like water

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33
Q

types of fats:

A

triglycerides
phospholipids
steroids

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34
Q

fats:

A

concentrated source of energy

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35
Q

lipids:

A
  • in cell membrane maintain fluidity
  • protection around organs and joints
  • surround neeve cellsnto speed up nerve impulse
  • insulates body
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36
Q

triglycerides:

A

fats made of glycerol + 3 molecules of fatty acid

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37
Q

fatty acids vary in:

A

vary in length and saturation

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38
Q

esterification reaction:

A

a reaction where each hydroxyl group of glycerol can connect to a fatty acid

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39
Q

fatty acids:

A

long hydrocarbon chains (w a carbonyl group on the end to make an acid)

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40
Q

OH groups from glycerol react w COOH groups from the fatty acid to…

A

form a fat through dehydration synthesis

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41
Q

steroids:

A

fats based on the structure of cholesterol

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42
Q

cholesterol is important in..

A

the structure of cell membranes (& in synthesis) of many hormones in the body such as testosterone, estrogen, aldoesteron, and more

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43
Q

high cholesterol levels in blood leads to..

A

leads to atherosclerosis

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44
Q

atherosclerosis:

A

a disease where plaque builds up inside your arteries

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45
Q

trans fat promotes:

A

-build up of plaque on arteries & cholesterols

bad cholesterols build up plaque

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46
Q

phospholipids:

A

phosphate based structure & 2 fatty acids (important in cell membrane structure)

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47
Q

phospholipids are similar to triglycerides but

A

1 fatty acid is replaced by a highly polarphosphate group

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48
Q

hydrophilic:

A

where water is attracted

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49
Q

essential amino acids…

A

8 of 20 can’t be synthesized by the human body so we MUST be supplied by food sources

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50
Q

proteins:

A

made of amino acids linked by covalent bonds (called peptide bonds)

51
Q

residue:

A

amino acids

52
Q

the sequence of amino acids is…

A

specific for each protein

53
Q

proteins primary structure:

A

long sequence of amino acids

54
Q

important roles of proteins:

A
  • enzymes
  • cell surface makers
  • cell membrane protein channels
55
Q

secondary, tertiary, and quaternary structures:

A

when 2 or more polypeptides join together and interact in specific way

56
Q

alpha helix (pleated sheet):

A

when a primary sequence of a protein can be folded on itself forming two visible secondary structures

57
Q

alpha helix (or pleated sheet) is held by:

A

hydrogen bond

58
Q

the tertiary structure:

A

the 3 dimensional globular structure

59
Q

what are tertiary structures held by?

A

interactions w amino acids, hydrogen bonds, and disulfide linkage

60
Q

quartenary structure

A

when 2 or more polypeptides join tighter and interact in specific ways

61
Q

allosteric site:

A

site separate from the active site

62
Q

proteins have a globular structure which…

A

is not rigid!

63
Q

globular structures..

A

are flexible and can often change shape

64
Q

when a substance binds to an allosteric site,….

A

the enzyme ⬆️’s or ⬇️’s the productivity of the enzyme

65
Q

how to shut down an enzyme:

A

to activate it or shut it down by having another molecule bind to the allosteric site to regulate its activity

66
Q

allosteric regulation:

A

changing the shape of an enzyme so the substrate can no longer fit the active site (other molecules fit into the allosteric site)

67
Q

enzymes:

A

protein molecules that act as biological catalysts

68
Q

catalyst:

A

provides surface to break bonds between the reactant molecules. then rearranges atoms in order to create binds to form the products

69
Q

if no catalyst is present…

A

reactant molecules must collide with enough energy (& correct orientation in order to break bonds)

70
Q

activation energy:

A

energy required to reach a state where reactant bonds are breaking and product bonds are forming (transition state)

71
Q

speeding up a chemical reaction can be done in a lab and not…

A

in a living system where organisms are made of proteins that will denature upon heating

72
Q

exergonic:

A

products that have a higher energy than reactants (system gives off energy)

73
Q

endergonic reaction:

A

products have a lower energy than reactants (system requires energy)

74
Q

in the lock and key theory phase 2 the enzyme…

A

slightly changes shape so when substrate enters, it precisely fits

75
Q

there are many different enzymes to catalyze all the different reactions and they are all..

A

specific to each substrate

76
Q

enzyme regulation:

A

enzyme activity needs to be controlled by cell.

- prevents unwanted accumulation of substrate and products.

77
Q

one method for controlling enzyme activity is through

A

the allosteric site (substance that binds to the allosteric site is often a product / substrate)

78
Q

when a certain product is needed, the substrate can ..

A

activate the enzyme by binding to the allosteric site and turning the enzyme on

79
Q

feedback inhibition:

A

when the cell turns off the enzyme by having the product molecule bind to the allosteric site. this gives enzyme feedback when there r high concentrations of product

80
Q

coenzymes

A

organic molecules

81
Q

cofactors

A

inorganic ions

82
Q

non protein substances such as coenzymes and cofactors…

A

work w an enzyme to help the enzyme function

83
Q

many vitamins from your diet work as ..

A

coenzymes

84
Q

many minerals from your diet work as..

A

cofactors

85
Q

inhibition:

A

enzymes can be inhibited in many different way

86
Q

the two general methods of inhibiting an enzyme:

A

competitive and non competitive inhibition

87
Q

competitive inhibition

A

another molecule other than the substrate competes for the active site of the enzyme

88
Q

when substrate concentration increases…

A

more substrate molecules are available to compete for the active site and overcome competitive inhibition

89
Q

non competitive inhibition

A

the inhibitor fits into another enzyme site other than the active site

90
Q

during the process of non comp inhibition

A

the shape of enzyme is altered and once changed, the substrate no longer fits into the active site (the enzyme cannot catalyze the reaction)

91
Q

what will not affect non comp inhibition

A

adding substrate

92
Q

the inhibitior molecule may release the allosteric site making …

A

non comp inhibition reversible as in the case of allosteric regulation

93
Q

if the inhibitor binds permanently (or permanently alters the enzyme shape) for comp inhibition…

A

it is non reversible

94
Q

cell membrane:

A

separates living cells from non living

- selectively permeable membrane surrounding the cell

95
Q

fluid mosaic model:

A

the cell membrane is a fluid mosaic of various macromolecules that are fluid (capable of motion) within the membrane

96
Q

proteins:

A

(found in plasma membrane) have various functions acting as channels such as receptor sites, connections, identification markers

97
Q

marker proteins: (peripheral)

A

rest on one side or the other of the membrane

98
Q

transport proteins: (integral proteins)

A

span both sides of the membrane

99
Q

diffusion:

A

movement of molecules from an area of high conversation to low concentration (molecules such as O and H2O move in and out of cell through diffusion) ex: perfume

100
Q

diffusion does not require:

A

energy to be expended by the cell. (a natural process)

101
Q

osmosis:

A

special type of diffusion.

movement of water from high concentration to low though a semipermeable membrane

102
Q

ex of osmosis:

A

water lines into cell where concentration is lower and expands blood cell

103
Q

hypertonic:

A

has a lower water concentrations outside vs inside cell

104
Q

hypotonic:

A

has more water outside than inside

105
Q

active transport:

A

carries molecules against a concentration gradient and requires cellular energy

106
Q

active transport uses..

A

a carrier protein

107
Q

molecules require energy supplied by

A

atp

108
Q

molecules move in opposite direction in active transport

A

than the natural occurring direction during diffusion

109
Q

atp

A

adenosine triphosphate (molecules that carries energy into cell)

110
Q

when the cell needs energy

A

atp is broken down

111
Q

atp is broken down by

A

removing a phosphate group and releasing the energy to where it is needed in the cell

112
Q

atp is the only form of energy…

A

cells can use. releases chemical energy

113
Q

bulk transport:

A

a way to get large molecules into or out of the call that cannot pass though the membrane or protein channel

114
Q

endocytosis:

A

used to transport material into the cell

115
Q

exocytosis

A

used to transport molecules such as proteins and cell products from inside cell to our

116
Q

3 types of endocytosis

A
  1. phagocytosis
  2. pinocytosis
  3. receptor-mediated endocytosis
117
Q

phagocytosis:

A

process where large molecules are brought into cell

118
Q

pinocytosis:

A

process where small molecules are brought into the cell

119
Q

receptor - mediated endocytosis:

A

requires a receptor (protein) to be activated for a vesicle to be made

120
Q

endocytosis molecules are dissolved:

A

in water or liquids

121
Q

exocytosis requires:

A

packaging from golgi of cellular products into a vesicle

- then merges and fuses w plasma membrane and is released it exyracellular fluid or bloodstream

122
Q

polypeptides:

A

chains of amino acids

123
Q

proteins are made of:

A

1 or more polypeptides molecules

124
Q

amino acids linked ..

A

covalently by peptide bonds

Bio: Grade 12 (4 decks)

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