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IB Biology > 2 - Chemistry of Life > Flashcards

2 - Chemistry of Life Flashcards

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1
Q

3 types of biological molecules

A
  • Carbohydrates
  • Lipids
  • Proteins
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2
Q

Most living things are made of these 3 elements

A

Carbon, hydrogen, oxygen

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3
Q

Why are life forms carbon based?

A

Carbon bonds with everything very easily

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4
Q

Important properties of water?

A
  • Universal solvent
  • Polar
  • Cohesive & adhesive
  • High specific heat capacity
  • Less dense when solid
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5
Q

What elements are carbohydrates made of?

A

Carbon, oxygen, hydrogen

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6
Q

Types of carbs and how they are classified

A

Classified by number of monomers

  • Monosaccharides
  • Disaccharides
  • Polysaccharides
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7
Q

Examples of each type of carb

A
  • Monosacccharides: Glucose, ribose
  • Disaccharides: Sucrose, lactose
  • Polysaccharides: Glycogen, starch, cellulose
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8
Q

Functions of carbs?

A
  • Primary respiratory substrate (glucose)
  • Energy storage (starch and glycogen)
  • Structural support (cellulose)
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9
Q

Properties of monnosaccharides

A
  • Sweet & soluble
  • One monomer
  • General formula: (CH2O)n
  • Form crystals
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10
Q

3 types of monosaccharides w/ examples

A
  • Triose (3n): Glyceraldehyde
  • Pentose (5n): Ribose, deoxyribose
  • Hexose (6n): Glucose, fructose
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11
Q

Different sturctures of glucose?

A

Chain and ring

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12
Q

How is ring glucose formed?

A

Carbons on opposite ends of the chain form a bond with an oxygen bridge

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13
Q

Difference between α-glucose and ß-glucose?

A

In α-glucose, the hydroxyl group is below the plane of the molecule

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14
Q

Is glucose a reducing or oxidizing sugar?

A

Reducing

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15
Q

Properties of disaccharides

A
  • Made of 2 monomers
  • E.g. maltose, lactose, sucrose
  • Sweet and soluble
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16
Q

How are disaccharides joined? How are they broken up?

A

Condensation reaction forms a glycosidic (1→4) bond of adjacent sugars. Process is reversed by hydrolysis.

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17
Q

What are maltose, sucrose and lactose made of?

A

Matose: 2 α-glucose
Sucrose: Glucsoe + fructose
Lactose: Glucose + galactose

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18
Q

How can a ß- and α-glucose bond?

A

The ß-glucose flips over so ydroxyl groups are both adjacent, below the plane of the molecule

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19
Q

Properties of polysaccharides?

A
  • Large, insoluble

- Polymers

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20
Q

3 main polysaccharides

A
  • Starch: Storage of energy in plants
  • Glycogen: Storage of energy in animals
  • Cellulose: Make up cell walls
21
Q

Composition of starch?

A
  • Amylose: long coiled chain of α-glucose

- Amylopectin: Shorter branched coiled chain of α-glucose

22
Q

Composition of cellulose?

A
  • Long chains of ß-glucose joined at 180°
  • Straight zig-zag, not curved helix
  • Hydrogen bonds present too
23
Q

Compostion of glycogen?

A

Short, branched chains of α-glucose

24
Q

Composition of lipids (triglycerides)?

A

Glycerol + three fatty acid chains joined by ester bonds

25
Q

Types of lipids

A
  • Oils: more unsaturated

- Fats: More saturated

26
Q

Functions/properties of lipids?

A
  • Energy reserves
  • Osmotically active (non-polar, can’t dissolve)
  • In respiration, glycerol (after hydrolysis) used
  • Highly reduced (make lots of water when respired)
  • Good insulators
27
Q

Structure of phospholipids?

A

Glycerol + 2 fatty acids + phosphate group

28
Q

Composition of proteins?

A
  • Made of many amino acids

- Made of nitrogen, carbon, hydrogen and oxygen

29
Q

Few functions of proteins?

A
  • Structure
  • Antibodies
  • Enzymes
  • Hormones
30
Q

How are amino acids bonded?

A

Peptide bonds formed by condensatioin reaction between amine group and carboxylic acid group of adjacent amino acids

31
Q

Types of proteins? How are they classified?

A

Classified by number of peptide bonds

  • Dipeptide
  • Polypeptide
32
Q

Levels of structure of proteins

A
  • Primary
  • Secondary
  • Tertiary
  • Quartenary
33
Q

Explain levels of protein structure

A
  • Primary: Order of amino acids
  • Secondary: Coiled long strings
  • Tertiary: Coils form 3D sturctures and fold
  • Quarternary: Tertiary structures joint together
34
Q

________ code for one amino acid

A

3 nitrogenous bases

35
Q

Types of secondary structure

A
  • α helix

- ß pleat

36
Q

Hydrogen bonds are easily broken by

A
  • low pH

- High temperatures

37
Q

Types of bonds in tertiary structure

A
  • disulphide bridges
  • ionic bonds
  • hydrogen bonds
  • hydrophobi/hydrophilic interactions
38
Q

Types of insulations by lipids

A
  • Thermal (skin)
  • Mechanical (major organs)
  • Electrical (myelin sheaths)
39
Q

How do ester bonds form?

A

Condensation recation b/w hydroxyl group of glycerol and carboxylic acid of fatty acids

40
Q

5 uses of lipids?

A
  • Insulation
  • Bile acids
  • Membrane component
  • Energy storage/source
  • Hormones
41
Q

Structure of fatty acids?

A

Saturated hydrocarbon chain with carboxylic acid at one end

42
Q

What groups are present in amino acids?

A
  • Amine group
  • Carboxylic acid group
  • R group
43
Q

What are enzymes?

A

They are proteins that act as biological catalysts

44
Q

Characteristics of enzymes

A
  • Globular proteins
  • Soluble (hydrophilic R-groups point outwards)
  • Each enzyme has a precise shape
  • Specific to substrate
45
Q

2 types of enzymes and processes used

A
  • Extracellular: Digestion, Decomposers

- Intracellular: Respiration, Photosynthesis

46
Q

Where do reactions occur in enzymes?

A

Active site

47
Q

Which part of the enzymes bind to the substrate?

A

R-groups of proteins bind

48
Q

What forms when enzyme binds to substrate, and what is it called after the reaction?

A

Enzyme-substrate complex changes to enzyme-product complex

49
Q

What factors affect enzyme activity?

A
  • pH
  • Temperature
  • Substrate concentration
  • Enzyme concentration
  • Inhibitors
  • Cofactors

IB Biology (6 decks)

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