Module 2: Foundations In Biology - Biological Molecules Flashcards

(131 cards)

1
Q

In a protein, what are the 4 main elements??

A

Carbon

Hydrogen

Oxygen

Nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

How many different types of amino acids are there??

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the smallest amino acid??

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the R group of Glycine??

A

Hydrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the R group of Cysteine

A

CH2-SH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What does an R group determine??

A

Determines properties and bonds that the amino acids form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Hydrophobic

A

Water repellent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Hydrophyllic

A

Water loving

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Peptide bonding

A

Two amino acids joined in a condensation reaction

The bond between them is a peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is a peptide bond formed between??

A

Amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the resulting compound of peptide bonding??

A

A dipeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

In peptide bonding when do the amino acids join??

A

Amino acids join when the amine and carboxylic acid groups connected to the central carbon atom react

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What happens to the hydroxyl in the carboxylic acid group during peptide bonding??

A

The hydroxyl in the carboxylic acid group of one amino acid reacts with a hydrogen in the amine group of another amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

When is a polypeptide formed??

A

When many amino acids are joined together by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

When a polypeptide is formed what is the reaction catalysed by??

A

Catalysed by the enzyme peptidyl transferase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Where can the enzyme peptidyl transferase be found??

A

In ribosomes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is the structure of proteins??

A

Proteins consist of one or more polypeptides arranged as complex macromolecules

All proteins contain the elements carbon, hydrogen, oxygen and nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What do many bonds lead to (structure of proteins))

A

Different types of bonds are formed and these bonds lead to the formation of long chain amino acids
These long chain amino acids fold into complex structures

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is the effect of having different sequences of amino acids??

A

Leads to different structures with different shapes being produced

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Why are shape specific proteins important??

A

Because the specific shapes of proteins are vital for the many functions proteins have within organisms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Primary protein structure

A

A sequence chain of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Which bonds are present in the primary protein structure??

A

Peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Secondary protein structure

A

Hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Which bonds are present in the secondary protein structure??

A

Hydrogen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Tertiary protein structure
Three dimensional folding pattern of a protein due to side chain interactions
26
What bonds are present in the tertiary protein structure??
Hydrogen bonds Ionic bonds Disulfide bonds
27
In cysteine what are disulfide bonds formed between??
Formed between two sulphurs
28
Quaternary protein structure
Protein consisting of more than one amino acid chain
29
Which bonds formed in the quaternary protein structure??
Hydrogen bonds Ionic bonds Disulfide bonds Hydrophobic/hydrophilic interactions
30
If the order of amino acids change what happens to the primary structure of the protein??
Primary structure changes Gives a different function
31
Where will the bonds be to maintain the quaternary structure??
Between polypeptide chains Hydrophilic interactions in the middle of the structure
32
Ionic bonds
Form between positively and negatively charged groups
33
How can ionic bonds be broken??
By high temperature or a change in ph
34
What are Disulphide bridges/bonds formed between??
Form between two cysteine amino acids
35
Disulphide bonds/bridges
Involves sharing electrons so is a covalent bond
36
Properties of a Disulphide bridge/bond
Strong bond, not broken by an increase in temperature or change in pH
37
Why do hydrophobic amino acids repel water??
They have non polar R groups
38
Which way will hydrophobic amino acids face??
Face into cytoplasm or tissue fluid So will face inwards Interact and cluster
39
Why do hydrophilic amino acids love water??
Because they have polar R groups
40
Which way will hydrophilic amino acids face??
Will face outwards into the tissue fluid or cytoplasm
41
What do hydrogen bonds form between??
Form between an electropositive H+ atom and an electronegative O- atom
42
How can hydrogen bonds be broken??
Can be broken by a high temperature or change in pH
43
Structure of a globular protein
Protein curls into a ball Hydrophobic R face in Hydrophilic R face out Soluble
44
Structure of a fibrous protein
Proteins form long strands Insoluble Very tough
45
Catalytic example of a globular protein
Enzymes such as amylase and lipase
46
Regulatory example of a globular protein
Hormones such as insulin
47
Transport example of a globular protein
Haemoglobin
48
Protective example of a globular protein
Antibodies
49
Structural example of a fibrous protein
Collagen
50
Structural example of a contractile protein
Actin, myosin
51
What is a prosthetic group??
A prosthetic group is a non-protein part which is permanently bound to the protein and is essential for its purpose
52
Structure of haemoglobin (globular protein)
2 identical chains called alpha chains 2 identical but different chains called beta chains Chains packed closely together
53
Problems with haemoglobin - sickle cell anaemia
Single point mutation recessive disease In a beta chain, causes amino acid substitution polar for valine 6th amino acid in chain
54
What are simple proteins
Simple proteins only contain amino acids in their structure
55
What are conjugated proteins
Conjugated proteins contain amino acids plus some other type of chemical molecule
56
Structural proteins: collagen
Found as strong non-elastic white fibres in tendons, cartilage and bone
57
Structural proteins - elastin
Found as yellow elastic fibres in ligaments and joint capsules
58
Structural proteins - keratin
Found as an impermeable protein in skin, hair, feathers, nails and hooves
59
What type of protein is haemoglobin
Globular
60
What type of protein is catalase
Globular
61
What type of protein is insulin
Globular
62
What type of protein is collagen
Fibrous
63
What type of protein is keratin
Fibrous
64
What type of protein is elastin
Fibrous
65
What is the shape of haemoglobin
Ball shape
66
What is the shape of catalase
Ball shape
67
What is the shape of insulin
Ball shape
68
What is the shape of the collagen
Strand shape
69
What is the shape of keratin
Strand shape
70
What is the shape of elastin
Strand shape
71
Number of polypeptide chains in haemoglobin
4
72
Number of polypeptide chains in catalase
4
73
Number of polypeptide chains in insulin
2
74
Number of polypeptide chains in collagen
3
75
Number of polypeptide chains in keratin
4
76
Number of polypeptide chains in elastin
Many
77
Is haemoglobin soluble or insoluble
Soluble
78
Is catalase soluble or insoluble
Soluble
79
Is insulin soluble or insoluble
Soluble
80
Is collagen soluble or insoluble??
Insoluble
81
Is keratin soluble or insoluble
Insoluble
82
Is elastin soluble or insoluble
Insoluble
83
Amino acid structure in haemoglobin
2 alpha chains 2 beta chains
84
Amino acid structure in collagen
Glycine every 3rd amino acid Glycine’s r group is hydrogen only Allows light coiling of polypeptide chains
85
Amino acid structure of keratin
Fibrous High proportion of cistane and Disulphide bonds
86
Amino acid structure of elastin
Cross links are covalent bonds between elastic fibres
87
Prosthetic group of haemoglobin
Haem - iron
88
Prosthetic group of catalase
Haem - iron
89
Prosthetic group of elastin
Many lysine can form covalent bonds
90
Prosthetic group of insulin
Doesn’t have one
91
Prosthetic group of collagen
Doesn’t have one
92
Prosthetic group of keratin
Doesn’t have one
93
Role of haemoglobin
Oxygen and carbon dioxide transport
94
Role of catalase
High conc found in liver Involved in breaking down h2o2 into water and oxygen
95
Role of insulin
Insulin lowers blood glucose concentration by converting glucose into glycogen
96
Role of collagen
Present in ligaments and tendons, skin, the outer layer of blood vessels Staggered ends to prevent weak points
97
Role of keratin
Found in hair and nails
98
Role of elastin
Elastic fibres in arteries, veins, arterioles, bronchioles and airways Can stretch and relax
99
Similarities between haemoglobin and catalase
Have a haem prosthetic group Have a 4o structure Are soluble Are globular 4 polypeptide chains Ball shaped proteins
100
Which elements do carbohydrates contain??
Carbon Hydrogen Oxygen
101
3 types of carbohydrates
Monosaccharide Disaccharide Polysaccharide
102
Examples of monosaccharides
Glucose Fructose Deoxyribose
103
Examples of disaccharides
Sucrose Lactose Maltose
104
Examples of polysaccharides
Starch Glycogen Cellulose
105
Alpha glucose structure
Hydrogen above the ring on C1
106
Beta glucose structure
H below the ring on C1
107
Colorimeter
Can record absorbable or transmission
108
Will a paler colour solution absorb more or less light
Absorb less light Therefore more light is transmitted
109
Will a darker coloured solution absorb more or less light
Absorb more light Therefore less light is transmitted
110
Where do you naturally find fructose
In fruit
111
What is the structural difference between ribose and deoxyribose
There is an extra oxygen molecule in ribose
112
What molecule is ribose found in?
RNA
113
What molecule is deoxyribose found in??
DNA
114
What type of bond joins 2 monosaccharides and what type of reaction is this??
Glycosidic bonds, condensation reaction
115
What is the effect of a glycosidic bond??
Creates a straight chain shape
116
What is a molecule of water made up of
2 hydrogen atoms, 1 oxygen atom which are joined by a covalent bond
117
Why is water a polar molecule
Electrons are not evenly shared in the covalent bond More of the electrons are pulled closer to the oxygen molecule giving it a relative delta negative charge and the hydrogens are delta positive
118
What bonds are present in water molecules
Hydrogen bonds and covalent bonds
119
Are hydrogen bonds weak or strong in water??
The bonds are weak In the liquid form water molecules move around and break and reform hydrogen bonds
120
Thermal stability of water - what happens with lower temperatures of water
With lower temperatures water molecules have less kinetic energy so more hydrogen bonds form and are less likely to break
121
What happens when water freezes??
On freezing, hydrogen bonds between water molecules form a lattice like structure This makes the water molecules more spread out
122
Why does ice float
Because the spread out water molecules are less dense than water in its liquid form
123
What are the advantages of water freezing to living organisms??
Insulated the water below Organisms below the ice survive by being able to move around and obtain food and oxygen Water currents still occur which moves nutrients The ice also provides a surface for organisms to live on
124
What is the effect of increasing water temperatures on water molecules??
Water molecules have more kinetic energy and move around more
125
What is required for evaporation to occur??
Hydrogen bonds between molecules must be broken which requires a lot of energy
126
What is high specific heat capacity
Energy needed to raise the temperature of one gram of substance by one degree Celsius
127
What is latent heat of evaporation
Amount of energy needed to break the hydrogen bonds between water molecules
128
Evaporation of water from the skin is an example of what??
Latent heat of evaporation
129
When does cohesion occur??
The hydrogen bonds between the molecules pulls the water together
130
What is the effect of surface tension??
Allows organisms to walk on water eg pond skaters and flies
131
Why is it important for water to be transparent
Allows light to penetrate through a body of water Facilitates photosynthesis of aquatic plants and allows predators to spot prey beneath the water above and for prey to see their predator