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Biol 1190 > lecture 2 > Flashcards

lecture 2 Flashcards

1
Q

everything is made of ______

A

matter

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2
Q

smallest unit of matter

A

atom

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3
Q

molecules are … (2)

A

a group of atoms

connected by covalent bonds

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4
Q

Compounds are … (3)

A

atoms connected by chemical bonds

in a fixed ratio

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5
Q

chemical bonds (3)

A

ionic bonds
covalent bonds
hydrogen bonds

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6
Q

covalent bond

A

when two atoms share one or more pairs of electrons

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7
Q

ionic bond

A

when a metal transfers one or more electrons to a nonmetal.

or

when two ions are held together by opposite charges

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8
Q

compound

A

a substance made of two or more different chemicals combined in a fixed ratio

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9
Q

water is … (

A

held by a polar covalent bond

when there are multiple, they are held by hydrogen bonds through electronegativity

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10
Q

water exhibits ______

what does it mean?

A

cohesion

molecules tend to stick to one another

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11
Q

why is water good at moderating temperature?

A

water takes a long time to heat up because before the molecules can move (heat up), the hydrogen bonds keeping them in place must be broken

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12
Q

why does water expand on freezing?

A

hydrogen bonds forces water into an orderly fashion called a lattice while freezing, making it less dense than water

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13
Q

polar

A

a molecule with a charge on one side that is not canceled out

or

a molecule that is not symmetrical

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14
Q

non polar

A

molecules with even charge distribution and symmetrical shape

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15
Q

hydrophilic

A

water loving - phosphate group

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16
Q

hydrophobic

A

water fearing - oil

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17
Q

acid

A

a substance that increases the H+ concentration in water

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18
Q

base

A

a substance that increases the concentration of OH- in water

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19
Q

buffer

A

substances that minimize change in pH

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20
Q

what pH must blood be kept between

A

7.35-7.45

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21
Q

what happens when blood pH falls below 7.35 or above 7.45

A

below - blood acidosis

above - blood alkalosis

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22
Q

what do organic molecules contain

A

carbon

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23
Q

carbon skeleton

A

carbons connected by covalent bonds in a chain or ring

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24
Q

functional groups

A

other atoms or molecules attaches to the carbon skeleton

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25
Q

hydroxyl

A
  • part of alcohols
  • polar
  • hydrophilic
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26
Q

sulfhydryl

A
  • part of thiols including amino acids
  • polar
  • hydophilic
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27
Q

carbonyl

A
  • part of ketones and aldehydes
  • polar
  • hydrophilic
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28
Q

carboxyl

A
  • part of carboxylic acids and amino acids
  • negatively charged (at body pH)
  • hydrophilic
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29
Q

ester

A
  • part of dietary fats, oils, triglycerides
  • aspirin is an example of an ester
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30
Q

phosphate

A
  • part of ATP and nucleic acids
  • very hydrophilic
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31
Q

Amino

A
  • part of amino acids
  • at body pH, positively charged
  • hydrophilic at body pH
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32
Q

different chemical structures lead to different chemical _____

A

properties

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33
Q

monosaccharides / simple sugars

A

monomers of carbohydrates

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34
Q

carbohydrates

A

compounds containing carbon, hydrogen, and oxygen.

major fuel for cells

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35
Q

dehydration synthesis

A

a process that takes away a water molecule and links two monosaccharides or amino acids

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36
Q

hydrolisis

A

breaking apart a disaccharide with water

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37
Q

glycosidic bond

A

the bond between monosaccharides after dehydration synthesis

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38
Q

disaccharides

A

molecules formed by joining two monosaccharides

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39
Q

polysaccharides

A

molecules made of many (100s-1000s) monosaccharides

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40
Q

types of glycosidic bond

A

alpha and beta

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41
Q

glycogen

A

bond type - alpha
structure - branched /compact
function - store energy in animals
example - muscle and liver cells

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42
Q

starch

A

bond type - beta
structure - long straight chain
function - store energy in plants
example - corn and potato cells

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43
Q

stereochemistry

A

3D arrangement of atoms and molecules

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44
Q

why can humans not break down starches?

A

humans do not possess the enzyme to break beta glycosidic bonds in starches, instead, they act as fibres to assist in digestion

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45
Q

lipids

A

hydrophobic molecules made of carbon, hydrogen, and a bit of oxygen. make up 18-25% of body mass in humans

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46
Q

types of lipids

A

fatty acids
triglycerides
phospholipids
steroids
eicosanoids
fat-soluble vitamins

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47
Q

fatty acids

A

hydrocarbon chain with a carboxyl group at one end

can be saturated of unsaturated

48
Q

saturated vs unsaturated fatty acids

A

saturated - contains only single covalent C-C bonds

unsaturated - contains one or more C-C double bonds
- will create a kink or bend in the chain

49
Q

triglycerides

A

three fatty acids bonded to a glycerol backbone by ester bonds

50
Q

fats vs oils

A

fats are triglycerides solid at room temp

oils are the same but liquid at room temp

51
Q

adipocytes

A

cells that store triglycerides

52
Q

saturated fats contain mostly _____

A

fatty acids

53
Q

unsaturated fats are either ______ or _______

A

monounsaturated or polyunsaturated

54
Q

monounsaturated fats examples

A

avocado, peanuts, olives

55
Q

polyunsaturated fats examples

A

corn, sunflower, fish oils

56
Q

phospholipids

A

glycerol backbone covalently linked to two fatty acids and a phosphate group

57
Q

Polar phosphate “head” of a phospholipid is _____

A

hydrophilic

58
Q

fatty acid “tails” of a phospholipid are _____

A

hydrophobic

59
Q

amphipathic

A

molecules with hydrophobic and hydrophilic parts

60
Q

steroids

A

formed by 4 fused carbon rings (cholesterol = starting molecule)

61
Q

sterols

A

steroids with at least one hydroxyl group

62
Q

what does the hydroxyl group do for sterols? why is it important?

A

having a hydroxyl group makes sterols amphipathic, allowing them to cross the phospholipid bilayer. It also allows them to be bound by blood proteins and transported in the blood

63
Q

eicosanoids

A
  • 20 carbon rings
  • includes prostaglandins and leukotrienes (immune signalling molecules)
64
Q

what is the monomer of lipids?

A

there is no monomer for lipids, structures are too diverse

65
Q

proteins

A

mainly made of carbon, hydrogen, oxygen, and nitrogen
make up 12-18% of body mass

66
Q

monomer of protein

A

amino acids

67
Q

how many amino acids are there?

A

20

68
Q

amino acids consist of: (4)

A

central carbon atom bonded to:
- amino group (left)
- carboxyl group (acid)(right)
- R group (top) (reactive side chain)

69
Q

peptide bond

A

a covalent bond found in amino acids

70
Q

dehydration synthesis and hydrolysis occur in:

A

carbohydrates (monosaccharides)
and
proteins (amino acids)

71
Q

peptide

A

a few amino acids joined together

72
Q

polypeptide

A

many (10-2000) amino acids joined together

73
Q

difference between a peptide and a protein?

A

small proteins can be a single polypeptide chain

large proteins can be many polypeptide chains folded in complex ways

74
Q

what determines protein function?

A

its structure

for reverse, what does structure determine in proteins?

75
Q

primary structure

A

amino acid sequence
determined by gene sequence
stabilized by peptide bonds

76
Q

secondary structure

A

repeated folds of proteins

could be alpha helicies (helix)
or
beta sheets (like folded paper)

77
Q

tertiary structure

A
  • 3D shape
  • determined by primary and secondary structure + bonds and forces that connects the chains
  • disulphide bridges between R groups stabilize
  • also supported by hydrogen and ionic bonds
78
Q

what determines 3D shape in protein folding?

A

hydrophobic interactions
primary/secondary structure

79
Q

quaternary structure

A
  • not in all proteins
  • the arrangement of polypeptide chains relative to others in multi-peptide proteins
80
Q

globular proteins

A

round and water soluble

81
Q

denaturing

A

when proteins lose their structure and are biologically inactive

82
Q

what denatures proteins?

A

pH, heat, heavy metals

83
Q

enzymes

A

biological catalysts

84
Q

cofactors

A

nonprotein molecules that assist enzymes

85
Q

coenzymes

A

cofactors that are organic molecules

86
Q

enzymes are: (3)

A

highly specific
efficient
regulated (cells control activity)

87
Q

active site

A

where chemical reactions are preformed on the enzyme

88
Q

proenzymes

A

inactive forms of enzymes that must be processed (usually a part must be cut off) to become active

89
Q

nucleic acids

A

encode genetic material

90
Q

nucleic acids

A

encode genetic material

made of carbon, hydrogen, oxygen, nitrogen, and phosphorus

can be either DNA or RNA

91
Q

DNA is ______ to RNA

A

transcribed

92
Q

RNA is _______ by ribosomes to proteins

A

translated

93
Q

nucleotides

A

monomer of nucleic acids
can be 1 of 3 things
- nitrogenous base
- pentose sugar
- phosphate group

94
Q

nitrogenous bases (5)

A

A - adenine
C - cytosine
T - thymine (in DNA)
G - guanine
U - uracil (in RNA)

95
Q

pentose sugars (2)

A

deoxyribose (in DNA)

or

ribose (in RNA)

96
Q

what are the biggest nitrogenous bases?

A

adenine and guanine are bigger than cytosine and thymine

97
Q

Purines (double ring bases)

A

Adenine and Guanine are:

98
Q

Pyrimidines (single ring bases)

A

Cytosol and Thymine are:

99
Q

nucleic acid pairing

A

A pairs with T

G pairs with C

100
Q

backbone of nucleic acid molecule consists of:

A

phosphate group + pentose sugar

101
Q

why is DNA shaped like a double helix?

A

due to the properties of the nucleotides

phosphate makes the backbone negative

102
Q

DNA is (general definition)

A

the genetic material of all living things

103
Q

how is DNA replicated?

A

double helix is opened, and each strand serves as a template for a new strand to be made off of

104
Q

semi conservative DNA replication

A

each daughter helix consists of one old and one new DNA strand (from the old double helix splitting)

105
Q

RNA types

A

mRNA - messenger
rRNA - ribosomal
tRNA - transfer

106
Q

mRNA

A

acts as the messenger between DNA and protein production

starts in nucleus, moves to ribosome

107
Q

tRNA

A

transports amino acids to ribosomes during translation

108
Q

rRNA

A

main component of a ribosome
provides a site for protein synthesis

109
Q

ATP

A

adenosine triphosphate

energy currency in cells

110
Q

Exergonic cellular reactions

A

reactions in which ATP is produced

111
Q

endergonic cellular reactions

A

reactions where ATP is consumes to do cellular work

112
Q

ATP structure

A

Adenine bonded to ribose bonded to a phosphate group

113
Q

how does ATP produce energy?

A

the terminal phosphate is broken off by an enzyme by hydrolysis. this leaves the ATP molecule as an ADP (adenosine DIphosphate), and releases a large amount of energy

114
Q

ADP

A

adenosine diphosphate

forms when the terminal phosphate is broken off of an ATP molecule

can become ATP again via synthesis with a catalyst

115
Q

catalyst for ADP to ATP reaction

A

ATP synthase

Biol 1190 (31 decks)

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