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Biological Molecules Flashcards

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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
Structure and find toons of plant cell wall?
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
26
What are bacterial cell walls made from?
Peptidoglycan
27
What's a lipid?
A group of substances that are soluble in alcohol rather than water. C H O Non polar
28
What's a macromolecule?
A very large organic molecule
29
What's a phospholipid?
Molecule consisting of glycerol, two fatty acids and one phosphate group
30
What is the structure of a triglyceride
Made of glycerol and fatty acids
31
Structure of glycerol?
3 carbons An alcohol 3 OH groups
32
Fatty acid structure?
Carboxyl group attached to hydrocarbon tail Carboxyl group can dissociate Creates H+ ion therefore acid
33
When is something saturated?
No double bonds
34
When is something unsaturated?
Double bond between 2 carbons One double bond - monounsaturated Multiple double bonds - polyunsaturated
35
Double bonds give fatty acids kinks. What do these kinks do?
Push the molecule apart slightly making it more fluid
36
How are ester bonds formed?
Condensation reaction of OH groups on a glycerol and fatty acid
37
5 functions of triglycerides
``` Energy source Energy store Insulation Buoyancy Protection ```
38
What's the structure of a phospholipid?
Same structure as triglyceride except one fatty acid is replaced by a phosphate group
39
What's a phospholipids behaviour in water?
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
Where will individual phospholipids move with a bilayer?
Around the layer but will not switch to the other side. Creates some stability
41
Why and what can pass through the phospholipid bilayer?
It's selectively permeable | Small non polar molecules
42
Define cholesterol
4 carbon based rings | Small hydrophobic molecule
43
What's cholesterols job?
Regulates fluidity
44
What's an amino acid?
Monomers of all proteins and all amino acids have the same basic structure.
45
What's a peptide bond?
Bond formed when two amino acids are joined by a condensation reaction
46
What are proteins and what are they're functions?
Large polymers compromised of amino acids Structural components eg muscles Enzymes antibodies hormones Carriers and pores
47
What elements do amino acids contain?
CHONS
48
How many amino acids are there?
20
49
What are on the ends of amino acids?
Amino group -NH2 | Carboxyl group -COOH
50
What enzymes breaks peptide bonds?
Protease
51
What is primary structure?
Sequence of amino acids found in a molecule
52
What is quaternary structure?
Protein structure where a protein consists of more than one polypeptide
53
What's secondary structure?
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
What's tertiary structure?
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
Where do hydrogen bonds form in amino acids?
Form in hydroxyl carboxyl and amino acid groups | Also between polar areas of the R groups on different amino acids
56
Where can ionic bonds form in an amino acid?
Between carboxyl and amino groups Positive and negatives attract to make an ionic bond
57
Where do disulfide links arise?
Between R groups of 2 cysteines. They are strong covalent bonds
58
What is a fibrous protein?
Has a relatively long, thin structure, is insoluble in water and metabolically inactive, often having a structural role within an organism
59
What's a globular protein?
Has molecules of a relatively spherical shape, which are soluble in water , and often have metabolic roles within the organism
60
What are prosthetic groups?
A non-protein component that forms a permanent part of a functioning protein molecule
61
Properties and function of collage.
``` Mechanical strength Withstands pressure in blood vessels Tendons Bones reinforced with calcium phosphate Cartilage and connective tissue ```
62
Properties and functions of keratin
Rich is cysteine therefore lots of disulfide bridges between polypeptide chains. Also h bonds. Very strong Nails hair horns waterproof and barrier
63
Properties of elastin
Cross linking and cooling make it strong and extensible. | Skin lungs and blood vessels
64
What is the quaternary structure of haemoglobin made up of?
2 a globin chains and 2 b globin chains
65
What do you call a protein associated with a prosthetic group?
Conjugated protein
66
Where does the oxygen bind to on haemoglobin
Iron in each of the 4 haem groups
67
What colour does haemoglobin turn when it binds to oxygen?
Purple red to bright red
68
Where do hydrogen bonds form in amino acids?
Form in hydroxyl carboxyl and amino acid groups | Also between polar areas of the R groups on different amino acids
69
Where can ionic bonds form in an amino acid?
Between carboxyl and amino groups Positive and negatives attract to make an ionic bond
70
Where do disulfide links arise?
Between R groups of 2 cysteines. They are strong covalent bonds
71
What is a fibrous protein?
Has a relatively long, thin structure, is insoluble in water and metabolically inactive, often having a structural role within an organism
72
What's a globular protein?
Has molecules of a relatively spherical shape, which are soluble in water , and often have metabolic roles within the organism
73
What are prosthetic groups?
A non-protein component that forms a permanent part of a functioning protein molecule
74
Properties and function of collage.
``` Mechanical strength Withstands pressure in blood vessels Tendons Bones reinforced with calcium phosphate Cartilage and connective tissue ```
75
Properties and functions of keratin
Rich is cysteine therefore lots of disulfide bridges between polypeptide chains. Also h bonds. Very strong Nails hair horns waterproof and barrier
76
Properties of elastin
Cross linking and cooling make it strong and extensible. | Skin lungs and blood vessels
77
What is the quaternary structure of haemoglobin made up of?
2 a globin chains and 2 b globin chains
78
What do you call a protein associated with a prosthetic group?
Conjugated protein
79
Where does the oxygen bind to on haemoglobin
Iron in each of the 4 haem groups
80
What colour does haemoglobin turn when it binds to oxygen?
Purple red to bright red
81
What chains are insulin made of?
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
What is Ab initio protein modelling ?
Model is built based on the physical and electrical properties of atoms in each amino acid. Multiple solutions
83
Comparative protein modelling
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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