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Biology🧪🌱💦 > Lecture 4 > Flashcards

Lecture 4 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

All living things contain what? (4)

A

nucleic acids, proteins, carbohydrates and lipids

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2
Q

Why is carbon so special? (2)

A
  • it can bound up with 4 separate atoms
  • it can bond with another C atoms
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3
Q

Is CO2 organic?

A

NO, it’s not organic b/c there’s only one C

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4
Q

Name 3 different arrangements of carbon skeleton:

A
  • straight
  • branched
  • rings (long or short) bonds
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5
Q

What are functional groups?

A

molecular commponents attached to that carbon skeleton

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6
Q

Name all 7 functional groups you need to know and recognize

A
  • Adelhyde
  • Carbonyl
  • Carboxyl
  • Phosphate
  • Hydroxyl
  • Sulfhydryl
  • Amino
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7
Q

You also have to know what 2 other functional groups

A

Estradiol and Testosterone

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8
Q

Biological molecules are composed of WHAT that are linked to each other

A

composed of subunits

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9
Q

How do you call a single unit?

A

a monomer (comme une perle)

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10
Q

How do you call a chain/ring of monomers?

A

a polymer (like a pearl necklace)

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11
Q

How do we build chains (polymers)? (2)

A

Dehydration Synthesis or Condensation reaction

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12
Q

What is this Dehydration Synthesis?

A

Dehydration removes a water molecule, forming a new bond
= a bond forms and WATER is released

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13
Q

How do you breakdown a chain (polymer)?

A

with hydrolysis

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14
Q

What is hydrolysis?

A

it adds a water molecule, breaking a bond
= water is added and a bond is broken

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15
Q

Name all 4 main classes of biological molecules

A
  • lipids
  • carbohydrates
  • proteins
  • Nucleix acid
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16
Q

Name a carbohydrate

A

sugar

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17
Q

could sugar be complex or simple

A

BOTH

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18
Q

What is the process of cellular respiration?

A

carbohydrates broken down for energy

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19
Q

How are they stored?

A

stored as long chains

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20
Q

Stored for long-term or short-term reserves?

A

short-term reserves

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21
Q

If there is too much of glycogen, what will happen?

A

the liver will store it

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22
Q

What are the 2 main functions of carbohydrates?

A
  • they serve as a source of energy (sugars)
  • they provide structure and support (cellulose)
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23
Q

In what ratio are C, H, O?

A

CH2O -> 1:2:1

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24
Q

Are monomers complex or simple sugars?

A

simple sugars (polymers are complex sugars)

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25
Q

What are the 2 types of simple sugars?

A
  • monosaccharides
  • dissacharides
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26
Q

What are monosaccarides?

A

monomers of carbohydrates

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27
Q

They share the same molecular formula, which one?

A

C6H12O6

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28
Q

Name 3 examples of monosaccharides

A
  • glucose
  • galactose
  • fructose
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29
Q

What are disaccharides?

A

2 linked monosaccharides

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30
Q

Give 3 examples of disaccharides

A
  • sucrose (glu. + fructose) (table sugar)
  • lactose (glu. glactose) (milk sugar)
  • maltose (glu. + glucose) (brewing sugar)
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31
Q

What are complex sugars named?

A

polysaccharides

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32
Q

What are polysaccharides?

A

polymers of monosaccharides

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33
Q

Name 2 storage carbohydrates

A
  • Starch
  • Glycogen
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34
Q

Starch is stored by what?

A

Energy storage in plants (where they convert excess glucose as starch)

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35
Q

Glycogen is stored by what?

A

animals stored excess glucose as glycogen

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36
Q

Name 2 structural carbohydrates

A

Cellulose and Chitin

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37
Q

Where can you find cellulose?

A

support in plants (wood) and fiber

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38
Q

Where can you find chitin?

A

in fungal cell walls and external skeleton of insects and other anthropods

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39
Q

TRUE OR FALSE:
Herbivores eat plants and produce enzymes

A

FALSE
they eat plants and DO NOT produce enzymes to breakdown cellulose

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40
Q

What is in their digestive system?

A

a house bacteria

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41
Q

Why does this bacteria have enzymes?

A

to breakdown cellulose

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42
Q

What is the second main class of biological molecules?

A

lipids

43
Q

Do lipids have water?

A

little or no affinity for water

44
Q

What are the 3 major types of lipids?

A
  • neutral fats
  • phospholipids
  • steroids
45
Q

TRUE OR FALSE
Different structures and functions but they are hydrophobic

A

TRUE

46
Q

what does hydrophobic mean?

A

water-fearing

47
Q

Long term or short term?

A

long-term reserves of fat tissue

48
Q

protections for vital organs from shock

A

TRUE

49
Q

buoyancy

A

TRUE (tendency of an object to float or to rise in a fluid when submerged)

50
Q

Does not maintain body temperature

A

FALSE it does

51
Q

Fat is constructed from what?

A

from 2 kinds of smaller molecules

52
Q

Define what these 2 kinds of smaller molecules are

A
  • 1 molecule of glycerol
  • 1 to 3 molecules of fatty acids
53
Q

There is a term that defines 3 fatty acids

A

triglyceride

54
Q

What is the second type of lipid?

A

A phospholipid

55
Q

are they a major constituent of cell membranes?

A

YES

56
Q

What is the structure of a phospholipid: (4é)

A
  • molecules similar to neutral fats
  • 2 molecules of fatty acids
  • 1 glycerol molecule
  • 1 phosphate molecule
57
Q

Phospholipids are an ________ molecule

A

amphipathic

58
Q

What does amphipathic mean?

A

it has hydrophobic and hydrophylic parts

59
Q

Which part is hydrophobic and which part is hydrophilic?

A

The HEAD is hydrophylic (attracted to water)
TAIL is hydrophobic (repelled from water)

60
Q

When placed in water, they self-assemble into what?

A

a bi-layer (double-layer)

61
Q

Is the head of the tail on the outside?

A

the hydrophilic head is outside
https://d20khd7ddkh5ls.cloudfront.net/lipids_phospholipids.jpg

62
Q

What is the third type of lipid?

A

steroids

63
Q

there are 3 main functions, name them

A
  • constituent of cell membrane (cholesterol)
  • components of vitamins (ex. vit. D)
  • components of hormones (ex. testosterone, estrogens, progesterone…)
64
Q

Steroids are made from what?

A

sterol

65
Q

What are sterols?

A

multiple rings of carbon atoms

66
Q

NEED TO RECOGNIZE A STEROL RING STRUCTURE AND A CHOLESTROL

A
67
Q

What are proteins known for?

A

proteins are the workhorses in the cell

68
Q

name all 4 main functions of a protein:

A

transport proteins
enzymes
protein hormones

69
Q

Proteins are made of what?

A

amino acids (monomers)

70
Q

All amino acids have the same basic skeleton, tell me important info

A
  • 20 commons a.a. used to build proteins
  • POLYPEPTIDES (polymer of a.a.)
  • PROTEIN (1 or more functional polypeptides)
71
Q

What do amino acids contain? (5)

A
  • carbon
  • hydrogen
  • oxygen
  • nitrogen
  • some of them also contain sulfur
72
Q

What is the basic strucutre of an amino acid?

A
  • 2 functional groups (amino group and carboxyl group)
  • 1 variable group (R)
73
Q

Name all 9 examples of a.a.

A
  • Glycine (Gly)
  • Alanine (Ala)
  • Valine (Val)
  • Leucine (Leu)
  • Isoleucine (Ile)
  • Methionine (Met)
  • Phenylalanine (Phe)
  • Tryptophan (Trp)
  • Proline (Pro)
74
Q

What is a polypeptide?

A

a chain of amino acids

75
Q

Name the process of water removal

A

Dehydration synthesis (condensation reaction)

76
Q

Going from a carboxyl group + amino group to a peptide bond
is that dehydration synthesis or hydrolysis?

A

Removal of h20 (water) so dehydration synthesis

77
Q

how levels are there to build a protein? name them

A

4 levels of stuctures
Primary
Secondary
Tertiary
Quaternary

78
Q

Why is the primary level so important?

A

b/c if the sequence and order of the a.a. is wrong, everything is wrong (which can lead to disease and abnormalities)

79
Q

Continue the sentence:
new form,

A

new function (form determines function)

80
Q

What can alter the protein’s conformation and ability to function?

A

every small change in the primary structure

81
Q

the order of the a.a. are determined by what?

A

by the nucleotide (genetically determined)

82
Q

Give an example of abnormality

A

a substitution of a single “wrong” a.a. in the primary structure can cause a disease sickle cell anemia
where blood cells don’t have the same shape (carries less oxygen = bad)

83
Q

What happens in the secondary structure?

A

coiling and folding of a sequence of amino acids

84
Q

Which 2 differents types of forms can they be coiled/folded

A

coiling –> alpha helix
folding –> beta pleated sheet

85
Q

The secondary structure of a protein is maintained by what type of bond?

A

Hydrogen bonds

86
Q

which type of form (alpha or beta) is common in fibrous protein?

A

beta pleated sheet (beta-keratin)

87
Q

are hydrogen bonds strong?

A

together, HB are strong
but weak individually

88
Q

Pleated sheets make up the core of what?

A

core of globular proteins

89
Q

Is tertiary related with a single or many polypeptides?

A

a SINGLE polypeptide

90
Q

Name 4 different kinds of bonds b/w a.a can occur within one protein

A

HB, ionic bonds, covalent bonds, hydrophobic interaction

91
Q

What is quaternary structure?

A

the fusion of 2 or more polypeptides (bond together) into one functional macromolecule

92
Q

Name 2 proteins and their structure

A

Hemoglobin –> 4 polypeptide subunits
Collagen –> 3 helical polypeptides

93
Q

What does Monomeric mean?

A

proteins made of a single polypeptide chain

94
Q

What does oligomeric mean?

A

2 or more polypeptide chains

95
Q

What do we call when the protein uncoils into a random shape

A

protein denaturation

96
Q

so what does protein denaturation mean?

A
  • disruption in 2 and 3 structures
  • temporary or permanent
    = break down of proteins
97
Q

True or false:
Denaturation reactions are strong enough to break a peptide bonds

A

FALSE

98
Q

What can break a peptide bond

A

high temperature

99
Q

Name a very important protein

A

a RIBOSOME

100
Q

in which structure are ribosomes displayed?

A

quaternary structure

101
Q

What does it use to make other proteins?

A

RNA

102
Q

Where are ribosomes made?

A

in the nucleolus

103
Q

HB a occur in which structures?

A

2 and 3 structures

104
Q

what can disrupt these bonds?

A

alcohol

Biology🧪🌱💦 (21 decks)

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