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Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What’s a hydrogen bond?

A

Weak interaction between slightly positively charged h atom and slightly negatively charged other atom

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2
Q

What’s a hydrolysis reaction?

A

When a molecule is split into two smaller molecules with the addition of water

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3
Q

What’s a monomer?

A

A small molecule which binds to many other identical molecules to form a polymer.

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4
Q

What’s a polymer?

A

A large molecule made from many smaller molecules called monomers

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5
Q

Why is water a good solvent?

A

The positive and negative parts are attracted to opposite charged parts of the solvent the water molecules cluster round the charges solvent parts and helps separate them and keep them apart( dissolved)

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6
Q

What are carbohydrates?

A

Group of molecules containing C, H and O

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7
Q

What is a glycosidic bond?

A

A bond formed between 2 monosaccharides by a hydrolysis reaction

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8
Q

What does hydrated carbon mean?

A

For every carbon there are 2 hydrogen and one oxygen atoms

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9
Q

What three functions do carbohydrates have?

A

Energy, energy store, structural units

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10
Q

Characteristics of monosaccharides

A

Sugars which taste sweet
Soluble in water
Insoluble in in non polar solvents
Straight chains, ring or cyclic forms

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11
Q

Sucrose is a … Sugar

Maltose and lactose are … Sugars

A

Non reducing

Reducing

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12
Q

A glucose + a glucose ->
A glucose +fructose ->
B galactose + a glucose ->
B glucose + b glucose ->

A

Maltose
Sucrose
Lactose
Cellobiose

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13
Q

Define homopolysaccharide

A

A polysaccharide solely made of one monosaccharide

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14
Q

Why are polysaccharides good energy stores?

A

Compact
Glucose can be snipped of chains
Branches tend to be more compact

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15
Q

What is amylase responsible for?

A

Hydrolysing 1-4 glycosidic linkages

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16
Q

What’s a condensation reaction?

A

When two molecules are joined together with the removal of water

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17
Q

Why are polysaccharides less soluble?

A

Hydrogen bonds are hidden away inside the molecule. This means the water potential is unaffected

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18
Q

What’s the structure of amylopectin?

A

Coiled into spiral shape
Hydrogen bonds holding spiral together
Hydroxyl group on c2 are on the inside making it less soluble and allowing h bonds to form

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19
Q

What is the structure of amylopectin?

A

Coiled into spiral shape which branches from c6

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20
Q

Glycogen structure?

A

Like amylopectin with more branches therefore more compact

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21
Q

Characteristics of cellulose?

A 
Tough
Insoluble 
Fibrous substance 
Homopolysaccharide 
Rotated b-glucose
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22
Q

Why doesn’t cellulose spiral?

A

Hydrogen bonds within the chain

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23
Q

What strengthens cellulose?

A

Hydrogen bonds between chains

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24
Q

How are macro fibrils formed?

A

About 70 cellulose chain -> microfibres

Up to 400 micro fibrils -> macro fibrils

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25
Q

Structure and find toons of plant cell wall?

A

Very high result strength
Macro fibrils cross cross for extra strength
Strength and support
Fully permeable
Prevents cell from bursting
Waterproof if reinforced with something else

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26
Q

What are bacterial cell walls made from?

A

Peptidoglycan

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27
Q

What’s a lipid?

A

A group of substances that are soluble in alcohol rather than water.
C H O
Non polar

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28
Q

What’s a macromolecule?

A

A very large organic molecule

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29
Q

What’s a phospholipid?

A

Molecule consisting of glycerol, two fatty acids and one phosphate group

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30
Q

What is the structure of a triglyceride

A

Made of glycerol and fatty acids

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31
Q

Structure of glycerol?

A

3 carbons
An alcohol
3 OH groups

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32
Q

Fatty acid structure?

A

Carboxyl group attached to hydrocarbon tail
Carboxyl group can dissociate
Creates H+ ion therefore acid

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33
Q

When is something saturated?

A

No double bonds

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34
Q

When is something unsaturated?

A

Double bond between 2 carbons

One double bond - monounsaturated

Multiple double bonds - polyunsaturated

35
Q

Double bonds give fatty acids kinks. What do these kinks do?

A

Push the molecule apart slightly making it more fluid

36
Q

How are ester bonds formed?

A

Condensation reaction of OH groups on a glycerol and fatty acid

37
Q

5 functions of triglycerides

A 
Energy source
Energy store 
Insulation 
Buoyancy 
Protection
38
Q

What’s the structure of a phospholipid?

A

Same structure as triglyceride except one fatty acid is replaced by a phosphate group

39
Q

What’s a phospholipids behaviour in water?

A

Phosphate group has a negative charge making it polar
Fatty acid tail are non polar
This makes the head hydrophilic and tail hydrophobic
Amphipathic
May form bilayer or micelles

40
Q

Where will individual phospholipids move with a bilayer?

A

Around the layer but will not switch to the other side. Creates some stability

41
Q

Why and what can pass through the phospholipid bilayer?

A

It’s selectively permeable

Small non polar molecules

42
Q

Define cholesterol

A

4 carbon based rings

Small hydrophobic molecule

43
Q

What’s cholesterols job?

A

Regulates fluidity

44
Q

What’s an amino acid?

A

Monomers of all proteins and all amino acids have the same basic structure.

45
Q

What’s a peptide bond?

A

Bond formed when two amino acids are joined by a condensation reaction

46
Q

What are proteins and what are they’re functions?

A

Large polymers compromised of amino acids
Structural components eg muscles
Enzymes antibodies hormones
Carriers and pores

47
Q

What elements do amino acids contain?

A

CHONS

48
Q

How many amino acids are there?

A

20

49
Q

What are on the ends of amino acids?

A

Amino group -NH2

Carboxyl group -COOH

50
Q

What enzymes breaks peptide bonds?

A

Protease

51
Q

What is primary structure?

A

Sequence of amino acids found in a molecule

52
Q

What is quaternary structure?

A

Protein structure where a protein consists of more than one polypeptide

53
Q

What’s secondary structure?

A

The coiling or folding of an amino acid chain, which arise often as a result of hydrogen bond formation between different parts of the chain. The main forms of secondary structure are the helix and the pleated sheet

54
Q

What’s tertiary structure?

A

The overall three dimensional shape of a protein molecule. It’s shape arise due to interactions including hydrogen bonds disulfide bridges ionic bonds and hydrophobic interactions

55
Q

Where do hydrogen bonds form in amino acids?

A

Form in hydroxyl carboxyl and amino acid groups

Also between polar areas of the R groups on different amino acids

56
Q

Where can ionic bonds form in an amino acid?

A

Between carboxyl and amino groups Positive and negatives attract to make an ionic bond

57
Q

Where do disulfide links arise?

A

Between R groups of 2 cysteines. They are strong covalent bonds

58
Q

What is a fibrous protein?

A

Has a relatively long, thin structure, is insoluble in water and metabolically inactive, often having a structural role within an organism

59
Q

What’s a globular protein?

A

Has molecules of a relatively spherical shape, which are soluble in water , and often have metabolic roles within the organism

60
Q

What are prosthetic groups?

A

A non-protein component that forms a permanent part of a functioning protein molecule

61
Q

Properties and function of collage.

A 
Mechanical strength 
Withstands pressure in blood vessels 
Tendons 
Bones reinforced with calcium phosphate 
Cartilage and connective tissue
62
Q

Properties and functions of keratin

A

Rich is cysteine therefore lots of disulfide bridges between polypeptide chains. Also h bonds. Very strong
Nails hair horns waterproof and barrier

63
Q

Properties of elastin

A

Cross linking and cooling make it strong and extensible.

Skin lungs and blood vessels

64
Q

What is the quaternary structure of haemoglobin made up of?

A

2 a globin chains and 2 b globin chains

65
Q

What do you call a protein associated with a prosthetic group?

A

Conjugated protein

66
Q

Where does the oxygen bind to on haemoglobin

A

Iron in each of the 4 haem groups

67
Q

What colour does haemoglobin turn when it binds to oxygen?

A

Purple red to bright red

68
Q

Where do hydrogen bonds form in amino acids?

A

Form in hydroxyl carboxyl and amino acid groups

Also between polar areas of the R groups on different amino acids

69
Q

Where can ionic bonds form in an amino acid?

A

Between carboxyl and amino groups Positive and negatives attract to make an ionic bond

70
Q

Where do disulfide links arise?

A

Between R groups of 2 cysteines. They are strong covalent bonds

71
Q

What is a fibrous protein?

A

Has a relatively long, thin structure, is insoluble in water and metabolically inactive, often having a structural role within an organism

72
Q

What’s a globular protein?

A

Has molecules of a relatively spherical shape, which are soluble in water , and often have metabolic roles within the organism

73
Q

What are prosthetic groups?

A

A non-protein component that forms a permanent part of a functioning protein molecule

74
Q

Properties and function of collage.

A 
Mechanical strength 
Withstands pressure in blood vessels 
Tendons 
Bones reinforced with calcium phosphate 
Cartilage and connective tissue
75
Q

Properties and functions of keratin

A

Rich is cysteine therefore lots of disulfide bridges between polypeptide chains. Also h bonds. Very strong
Nails hair horns waterproof and barrier

76
Q

Properties of elastin

A

Cross linking and cooling make it strong and extensible.

Skin lungs and blood vessels

77
Q

What is the quaternary structure of haemoglobin made up of?

A

2 a globin chains and 2 b globin chains

78
Q

What do you call a protein associated with a prosthetic group?

A

Conjugated protein

79
Q

Where does the oxygen bind to on haemoglobin

A

Iron in each of the 4 haem groups

80
Q

What colour does haemoglobin turn when it binds to oxygen?

A

Purple red to bright red

81
Q

What chains are insulin made of?

A

Two polypeptide chains
A chain starts with section of a helix. B chain ends with a section of b pleat. Folded into tertiary structure joined together by disulfide links.
R groups are on the outside making it soluble
Bind to glycoproteins receptors on fat and muscle cells to increase their glucose uptake

82
Q

What is Ab initio protein modelling ?

A

Model is built based on the physical and electrical properties of atoms in each amino acid.
Multiple solutions

83
Q

Comparative protein modelling

A

Protein threading scans amino acid sequence against a database of solved structures and produces a set of possible results

Biology (6 decks)

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