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Module 2.2 Flashcards

Biological molecules

1
Q

Why can water hydrogen bond

A

Oxygen has more protons in its nucleus than hydrogen (more electronegative)
The shared electrons are attracted slightly towards the oxygen nucleus
The oxygen becomes delta negative
Hydrogen becomes delta positive
H bonds between hydrogen and oxygen of separate molecules

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2
Q

Properties of water from H bonds

A

High SHC
Density
High latent heat of vaporisation
Adhesion and cohesion
Solvent
Liquid

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3
Q

Why is high SHC good

A

It is difficult to heat water up
provides stable habitat
Stable temperature for enzymes

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4
Q

Why is high latent heat of vaporisation good

A

Helps with cooling from sweat/panting

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5
Q

Why is density good

A

Ice is less dense than water
Difficult for whole bodies of water to freeze (animals can live under the ice)
Ice acts as an insulating layer (stable environment underneath)
Floating ice is habitat for other animals

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6
Q

Why is a solvent good

A

Transport medium
Substances dissolved in it can react (cytoplasm)

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7
Q

Why is adhesion and cohesion good

A

In the xylem
surface tension provides habitats for insects (pond skaters)

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8
Q

Why is liquid good

A

Transport medium
dissolved substances can move around

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9
Q

What is a monomer

A

the subunit(s) used to form a polymer when more than one is joined together

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10
Q

What is a polymer

A

A molecule consisting of more than one molecule joined together

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11
Q

What is a condensation reaction

A

The joining of two molecules
Water is removed

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12
Q

What is a hydrolysis reaction

A

The breaking apart of molecules
Uses up water

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13
Q

Element in carbohydrates

A

C,H,O

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14
Q

Elements in proteins

A

C,H,O,N,S

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15
Q

Elements in lipids

A

C,H,O

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16
Q

Elements in nucleic acids

A

C,H,O,N,P

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17
Q

Structure of amylopectin

A

Formed of a-glucose monomers
Branched 1-4 and 1-6 bonds
in a spiral shape
insoluble

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18
Q

Amylose structure

A

Formed of a-glucose monomers
Not branched 1-4 bonds only
Coiled
insoluble

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19
Q

Glycogen structure

A

Formed of a-glucose monomers
Highly branched 1-4 and 1-6 bonds
Less coiled
Insoluble

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20
Q

Cellulose structure

A

Formed of b-glucose monomers
straight chains because of OH on top in b-glucose
Alternating monomer are rotated 180
Can H-bond between chains
Insoluble

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21
Q

Function of glycogen, amylose and amylopectin

A

Energy storage glycogen=animals starch (amylose and amylopectin) = plants
Insoluble as OH group on inside of coil so don’t affect the water potential of the cells
Amylopectin and glycogen are branched to provide more hydrolysis points to remove glucose from the molecule (more energy per unit time)
Glycogen in most branched as it is in animals which are more metabolically active
Compact so don’t take up space
Glucose easily snipped off

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22
Q

Monomers of sucrose

A

Fructose and glucose

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23
Q

Monomers of maltose

A

2 glucose molecules

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24
Q

Monomers of lactose

A

galactose and glucose

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25
Triglyceride monomers
Glycerol, 3 fatty acids
26
Phospholipid monomers
Glycerol, phosphate, 2 fatty acids
27
difference between saturated and unsaturated fatty acids
Saturated have the maximum C-H bonds Unsaturated have one or more double C bonds so have a kink Kink means unsaturated are more liquid as tails means it is harder to compress into a liquid
28
Bond name between 2 or more monosaccharides
Glycosidic bond
29
Bond name between glycerol and fatty acids
Ester bond
30
Triglyceride function
Buoyancy Protection of organs Insulation (heat and electrical) Energy storage (insoluble) Energy source (can produce 2x as much energy as glucose)
31
Phospholipid function
Phosphate head is hydrophilic Fatty acid tails are hydrophobic Make up the plasma membrane (partially permeable as only small non-polar molecules can pass through tails)
32
Cholesterol structure
4 carbon based rings
33
Cholesterol function
Regulates fluidity of the plasma membrane Makes up steroid hormones Is hydrophobic
34
Bond name between amino acids
Peptide bonds
35
Primary protein structure
The sequence of amino acids Peptide bonds
36
Secondary protein structure
Initial folding Alpha-helix (mainly globular) Beta-pleated sheet (Mainly fibrous) Hydrogen bonds
37
Tertiary protein structure
Folding into 3D shape Hydrophobic/philic interactions (group together, phobic go inside philic go outside of molecule) Disulphide bridges (only between cysteine) Ionic bonds H bonds
38
Quaternary protein structure
Only in some proteins Joining of more than one polypeptide molecules
39
Structure of haemoglobin
2 globin chains 2 globin chains 4 haem groups (contains Fe+ ion) (prosthetic group)
40
Function of haemoglobin
Haem group bonds with oxygen to transport it in the blood to respiring tissues
41
Structure of insulin
2 polypeptide chains alpha chain starts with a-helix Beta chain ends with b-pleated sheet
42
Insulin function
Controls blood sugar by binding to glycoprotein receptors on cells to increase their uptake of glucose from the blood Soluble so can travel in the blood
43
What is a conjugated protein
Globular protein with a prosthetic group e.g. haemoglobin
44
Collagen properties
Mechanical strength
45
Collagen function
Around artery walls to prevent bursting Tendons Bonds Cartilage and connective tissues
46
Keratin properties
Insoluble and impermeable very strong
47
Keratin function
Impermeable barrier to infection Prevents entry of water-borne pollutants Mechanical protection
48
Elastin properties
Strong Extensible
49
Elastin function
Stretch and recoil of skin, bladder and alveoli Helps blood vessels stretch and recoil maintaining blood pressure
50
What does biuret test for
Proteins
51
Biuret positive result
Blue to lilac
52
How to carry out biuret test
Add sample to a spotting tile Add biuret
53
What does benedict's solution test for
Reducing sugars
54
Benedict's positive result
Blue to green/yellow/orange/brick red depending on concentration of reducing sugar
55
How to carry out benedict's test
Add sample to a test tube Add benedict's solution Heat in a water bath to at least 80 degrees for 3 mins
56
How to test for non-reducing sugars
Do normal benedict's test first Add sample to test tube Add hydrochloric acid to sample Heat in a water bath to a boil Neutralise with sodium hydrogen carbonate until fizzing stops Add benedict's solution Heat to at least 80 degrees
57
What does iodine test for
Starch
58
Iodine positive result
Yellow to blue/black
59
How to carry out starch test
Add sample to spotting tile Add iodine
60
What does emulsion test for
Lipids
61
Emulsion test positive result
White cloudy layer on top of solution
62
How to carry out emulsion test
Add sample to test tube mix sample with ethanol filter Pour solution into water leave to settle
63
How to determine concentration of substance - colorimetry
serial dilution of known concentration Set colorimeter to red Calibrate with distilled water Test absorption for known concentrations Plot calibration curve Test absorption for unknown Find absorption for unknown on calibration curve then down to concentration
64
R value calculation
Distance moved by the solute / distance moved by the solvent
65
Cellulose cell wall function
Plant cell walls High tensile strength prevents cells from bursting when turgid Criss cross wall for extra strength Space between microfibrils making it fully permeable for water and mineral ions to pass through Cellulose embedded in pectin Can be reinforced with waxes (suberin, cutin) for waterproofing
66
Pepsin structure
Single polypeptide chain Has very few basic R-groups Mainly acidic R-groups so is stable in the stomach as acidic R-groups cannot accept H+ ions
67
Pepsin function
Digests protein In the stomach

Biology (25 decks)

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