Biological molecule 2 (Proteins and Lipids) Flashcards

1
Q

Elements in lipids

A

Carbon, hydrogen and oxygen but they have a high proportion of H

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2
Q

Structure of triglycerides

A

One glycerol (alcohol) and three fatty acids

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3
Q

Saturated

A

No double bonds between carbon atoms, most likely to be solid at room temperature

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4
Q

Mono-unsaturated

A

One double bond between C atoms

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5
Q

Polyunsaturated

A

More than 1 double bond between C atoms, they cause the molecule to bend and can not pack closely together making them liquid at room temperature

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6
Q

Fatty acid tails

A

Made of hydrocarbons, they are hydrophobic making lipid insoluble in water

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7
Q

Basic fatty acid structure

A

Long hydrocarbon tails containing a carboxylic acid at one end

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8
Q

Forming a triglyceride

A

The hydroxyl groups interact leading to the formation of 3 water molecules and bonds between the fatty acid and glycerol molecule known as ester bonds in a process called esterification

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9
Q

What type of reaction is esterification?

A

Condensation reaction

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10
Q

What properties does the fatty acid tail give the triglyceride?

A

Density, melting point and sate at room temperature

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11
Q

Phospholipid structure

A

Glycerol, 2 fatty acids and a phosphate group

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12
Q

Is a phosphate group polar?

A

Yes

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13
Q

What does the polar nature of the phosphate group cause?

A

The head of the phospholipid is attracted to water (hydrophilic)

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14
Q

Non-polar fatty acid tail

A

Hydrophobic

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15
Q

Define amphipathic

A

Both hydrophobic and hydrophilic regions

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16
Q

Functions and properties of triglycerides

A
  1. energy storage molecules in animals and plants
  2. insoluble, they bundle into insoluble droplets with hydrophilic heads facing outwards
  3. long hydrocarbon chains contain a lot of chemical energy (twice as much per g as carbohydrates)
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17
Q

Phospholipid functions

A

cell membranes

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18
Q

Cholesterol functions

A

Strengthen the cell membrane by interacting with the phospholipid bilayer, making it less fluid and more rigid

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19
Q

Functions of lipids

A
  1. Plasma membrane
  2. energy store
  3. absorption of fat soluble vitamins (A,E,D,K)
  4. myelin sheath around axons
  5. energy store, protection and buoyancy
  6. source of water (respiration)
  7. water proofing
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20
Q

Test for lipids

A

Emulsion test - shake the substance with ethanol, shake, add to water and a milky colour will indicate a lipid

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21
Q

Elements in proteins

A

Carbon, hydrogen, oxygen and smaller quantities of nitrogen and sulphur

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22
Q

Protein monomers

A

Amino acids

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23
Q

Functions of proteins

A
  1. structural
  2. catalytic
  3. signalling
  4. immunological
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24
Q

General structure of proteins

A

Amino group, carboxylic acid group and ‘R group’

25
Carboxyl group
COOH
26
Amino group
NH2
27
R group
Can be variable, simple as a H to a more complex ring structure
28
Protein synthesis
Long chains of amino acids joined together in a condensation reaction to from peptide bonds between individual amino acid monomers
29
Peptide bond (C-N)
Covalent bond between the C (from the carboxylic acid) and the N (from the amino group)
30
4 structural levels of protein
1. Primary 2. secondary 3. tertiary 4. quaternary
31
Primary structure
1. The sequence of amino acids in the polypeptide chain 2. no IM bonds or interactions 3. different proteins have different sequences
32
Secondary structure
1. Hydrogen bonds form between near by amino acids in the chain 2. this causes them to coil into an alpha helix or beta pleated sheet 3. thus they are no longer flat
33
Tertiary structure
1. The coiled chain is coiled further 2. more bonds form between different parts of the polypeptide chain 3. forms the final 3D structure (for proteins made of one chain)
34
Bonding in the tertiary structure
1. hydrophobic/hydrophilic interactions 2. hydrogen bonds 3. ionic bonds 4. disulphide bridges
35
Quaternary structure
1. The way in which the polypeptide chains are assembled together 2. more than 1 polypeptide chain for subunit 3. NOT all proteins have a quaternary structure 4. influenced by all bonds above 5. prosthetic group
36
What causes denaturation of proteins?
Changes in temperature, PH or salt concentration
37
Fibrous protein shapes
Long unbranched, parallel chains
38
Fibrous protein function
Support and structural
39
Fibrous protein sequence of amino acids
Repetitive and regular
40
Fibrous protein stability / sensitivity to temperature
Stable
41
Fibrous protein examples
Collagen, keratin
42
Globular protein shape
Spherical (chains folded)
43
Globular protein fucntions
Metabolic (enzymes)
44
Globular protein solubility in water
Soluble
45
Fibrous protein solubility in water
Insoluble
46
Globular protein sequence of amino acids
Irregular
47
Globular protein stability / sensitivity to temperature
Unstable
48
Globular protein exmaples
All enzymes, some hormones (e.g insulin) and haemoglobin
49
Haemoglobin
1. Carries O2 around the body in red blood cells 2. conjugated protein (a non-protein group attached) 3. non-protein part is called a prosthetic group = Heam group containing iron
50
Insulin
1. Hormone secreted by the pancreas 2. regulates the blood glucose levels 3. soluble meaning it can be easily transported in the blood
51
Insulin structure
Two polypeptide chains, held together by disulphide bridges
52
Amylase
1. enzyme - breakdown of starch | 2. single chain of amino acids
53
Collagen
1. found in animal connective tissues 2. mineral bind to increase rigidity 3. strong
54
Keratin
Found in external structures of animals (hair, nails and skin, feathers and horns)
55
Elastin
Found in elastic connective tissue such as skin, large blood vessels and some ligaments
56
Biuret test for proteins
1. add a few drops of sodium hydroxide to turn the solution alkaline 2. then add a few drops of copper (II) sulphate solution 3.
57
Positive Biuret test result
Purple
58
Negative Biuret test
Remain blue (due to copper ions)