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OCR Biology > 2.2 BIOLOGICAL MOLECULES > Flashcards

2.2 BIOLOGICAL MOLECULES Flashcards

1
Q

Describe a water molecule (2)

A
  • Polar
  • Weak hydrogen bonding
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2
Q

State and explain the 4 properties of water

A

1) Solvent (water is polar so dissolves molecules)
2) Transport medium (can carry polar substances and is cohesive)
3) Coolant (high specific heat capacity and large latent heat of vaporisation)
4) Habitat (high specific heat capacity so acts as a buffer, cohesion creates surface tension for bugs, ice less dense than water so is insulator)

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3
Q

What elements are carbohydrates,lipids,proteins and nucleic acids made of?

A

carbohydrates - C,H,O
lipids - C,H,O
proteins - C,H,O,N,S
nucleic acids - C,H,O,N,P

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4
Q

What kind of reaction bonds together monosaccarides into a disaccaride?

A

Condensation (water removal)

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5
Q

What kind of reaction splits up a dissacharide back into its monosaccarides?

A

Hydrolysis (addition of water)

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6
Q

Draw alpha and beta glucose

A

Alpha has hydrogen above, Beta has hydrogen below

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7
Q

What type of bond forms between disaccharides and polysaccarides after condensation?

A

Glycosidic bond

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8
Q

How is the disaccharide MALTOSE formed?

A

(a)-GLUCOSE + (a)-GLUCOSE

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9
Q

How is the disaccharide LACTOSE formed?

A

(a)-GLUCOSE + GALACTOSE

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10
Q

How is the disaccharide SUCROSE formed?

A

(a)-GLUCOSE + FRUCTOSE

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11
Q

How are polysaccarides formed from monosaccarides?

A

via many condensation reactions (water removal)

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12
Q

Name the three polysaccarides.

A
  • Starch (amylose and amylopectin)
  • Cellulose
  • Glycogen
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13
Q

Describe glycogen (4)

A
  • energy SOURCE material in animals
  • C1 to C4 and C1 to C6 glycosidic bonds
  • alpha glucose
  • large surface area and densely packed
  • branched
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14
Q

What are the two types of starch?

A

amylose and amylopectin

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15
Q

Describe amylose starch (5)

A
  • energy STORAGE material in plants
  • C1 to C4 glycosidic bonds
  • alpha gluocse
  • densely packed
  • insoluble
  • branched
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16
Q

Describe amylopectin starch (5)

A
  • energy STORAGE material in plants
  • C1 to C6 glycosidic bonds
  • alpha glucose
  • large surface area
  • insoluble
  • branched
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17
Q

Describe cellulose (5)

A
  • a structural component in plant cell walls
  • C1 to C4 glycosidic bonds
  • beta glucose
  • long/straight/unbranched
  • hydrogen bonds
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18
Q

The three types of lipids

A
  • Triglyceride
  • Phospholipid
  • Cholesterol
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19
Q

Explain the solubility of lipids

A
  • insoluble in water because they are nonpolar/uncharged
20
Q

How to make triglycerides?

A
  • one glycerol
  • three fatty acids
  • esterification to form ester bonds
21
Q

Uses of triglycerides?

A
  • as an energy source (broken down to release energy during respiration)
  • as an energy store (insoluble so no effect on cells water potential)
  • keeping animals afloat (its less dense than water)
  • insulation/protection
22
Q

Structure of phospholipids?

A
  • one glycerol
  • two fatty acids (one saturated, one unsaturated)
  • one phosphate group
23
Q

Describe the phospholipid bilayer (3)

A
  • hydrophobic tails (polar, water soluble)
  • hydrophilic heads (nonpolar, insoluble)
  • selectively permeable (to small nonpolar molecules)
24
Q

Describe the properties and uses of cholesterol (2)

A
  • small and hydrophobic
  • sits in membrane phospholipid bilayer to regulate membrane fluidity
25
Q

General structure of an amino acid?

A
  • NH2 amine group
  • COOH carboxyl group
  • R variable group
  • H hydrogen group
26
Q

How are dipeptides/polypeptides formed?

A
  • two amino acids
  • condensation to form a peptide bond (water removal)
27
Q

How are dipeptides/polypeptides broken?

A
  • hydrolysis to break peptide bond (addition of water)
28
Q

State the levels of protein structure

A

Primary - the sequence of amino acids in the polypeptide chain
Secondary - alpha helix or beta pleated sheet
Tertiary - 3D shape
Quaternary - proteins with more than one polypeptide chain

29
Q

Explain primary structure of proteins

A
  • the unique sequence of 20 different amino acids in the polypeptide chain
30
Q

Explain the secondary structure of proteins

A
  • the hydrogen bonds between carboxyl and amine groups of amino aicds of the polypeptide chain fold it into either alpha helix or beta pleated sheet
31
Q

Explain the tertiary structure of proteins

A
  • unique 3D structure formed by; hydrophobic/hydrophillic interactions, hydrogen bonds, ionic bonds, disulfide links (all between R variable groups)
32
Q

Explain the quaternary structure of proteins

A
  • proteins with more than one polypeptide chain have a quaternary structure (e.g haemoglobin)
33
Q

State the two types of proteins

A

Globular and Fibrous

34
Q

State and explain the two globular proteins

A
  • insulin (metabollic protein)
  • haemoglobin (4 pp chains, 2 alpha, 2 beta, conjugated , 4 haem Fe2+ prosthetic groups)
35
Q

State and explain the three fibrous proteins

A
  • collagen (mechanical strength in skin)
  • keratin (skin/hair/nails)
  • ellastin (flexibility/elasticity in blood vessels)
36
Q

Describe globular proteins (3)

A
  • complex (quaternary)
  • spherical
  • water soluble
37
Q

Describe fibrous proteins (3)

A
  • strong
  • insoluble
  • not complex
38
Q

Chemical test for proteins?

A
  • add drops of biuret solution
  • BLUE to PURPLE
39
Q

Chemical test for starch

A
  • add drops of iodine
  • BROWN to BLUE/BLACK
40
Q

Chemical test for lipids

A
  • add ethanol, shake, pour extract into water
  • COLOURLESS to WHITE EMULSION
41
Q

Name the only non-reducing sugar

A

Sucrose

42
Q

Chemical test for reducing sugars

A
  • add benedicts reagent, heat 80 degrees
  • BLUE to BRICK RED
43
Q

Chemical test for non-reducing sugar (sucrose)

A
  • do the reducing sugar test first (benedicts and heat)
  • boil with HCl then cool and neutralise with NaOH
  • repeat benedicts test
  • BLUE to BRICK RED
44
Q

What can reagent test strips test for?

A
  • Can identify presence of reducing sugars by dipping into test solution and determine concentration when compared to calibration card
45
Q

What do colorimeters and biosensors do?

A
  • obtains quantitative results for the concentration of each biochemical test
46
Q

State the 5 steps of how to use a colorimeter

A

1) Zero the colorimeter
2) Add red filter
3) Calibrate using distilled water
4) Insert different known concentrations (e.g of glucose with benedicts solution) with serial dilutions
5) measure percentage transmission of light and create calibration curve

OCR Biology (27 decks)

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