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Macromolecules Flashcards

1
Q

Macromolecules (Biological Molecules)

A

4 organic (carbon-based) compounds are the building blocks of all living things:
- carbohydrates
- lipids
- proteins
- nucleic acids

Functions:
- energy storage
- insulation
- growth
- repair
- communication
- transfer of hereditary information

Bigger molecule = more carbon bonds = more energy

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2
Q

Another name for macromolecules

A

Polymers - large molecules

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3
Q

What are polymers composed of?

A

Subunits called monomers

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4
Q

How are polymers joined?

A

Through an enzymatic reaction, where a water molecule is removed

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5
Q

Carbohydrates

A

(CH2O)n [n=# of carbon atoms]
- short and long term energy storage
- energy extracted through CELLULAR RESPIRATION

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6
Q

Monosaccharides

A

Simple Sugars: ring molecule with 3-7 C atoms
- in the foods we eat

  • each containing 6 carbons are isomers
    C6H12O6
    Glucose, Galactose, Fructose
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7
Q

Alpha Glucose

A

Link to form glycogen and starch
OH at positions 1 and 4 are in the same position

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8
Q

Beta Glucose

A

Link to form cellulose
OH at positions 1 and 4 on opposite sides

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9
Q

Disaccharides

A

Double Sugars: 2 monsaccharides bonded together

C12H22O11 (CnH2On - H2O)

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10
Q

How are disaccharides formed?
What bond is formed?

A

Through a dehydration reaction
Glycosidic bond

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11
Q

Sucrose

A

In foods

Glucose + Fructose

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12
Q

Lactose

A

Dairy

Beta Galactose + Glucose = Alpha Lactose
Beta (1-4) glycosidic bond

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13
Q

Maltose

A

Starch

Glucose + Glucose

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14
Q

Lipids

A
  • LONG TERM energy storage
  • cushioning of organs (shock absorber)
  • chemical messengers (HORMONES)
  • insulation
  • 1g lipid stores 2.25x more energy than 1g carbohydrates
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15
Q

Lipid polarity

A

Nonpolar - insoluble in polar solvent - hydrophobic

Cannot form H bonds with water

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16
Q

Triglyceride

A

Glycerol + 3 fatty acids
Function: energy

Ex. fats (butter)

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17
Q

Fats

A

Triglyceries made through an esterification reaction

18
Q

Saturated fats

A
  • contain the maximum number of C-H bonds
  • solid at room temperature (i.e. animals fats, butter)
  • RICHER ENERGY source
19
Q

Unsaturated fats

A
  • do not have the maximum number of C-H bonds (C=C)
  • lower mp and bp
  • liquids at room temperature (i.e. plant oil)
20
Q

Phospholipids

A

Phosphate, fatty acids, phosphorilated alcohol
Function: (selective) barrier

Ex. cell membrane

21
Q

Steroids

A

Ring structures
Function: hormones (messangers)

Ex. testosterone, estrogen, cholesterol

22
Q

Terpenes

A

Amphiphilic
Function: pigment

Ex. chlorophyll

23
Q

Waxes

A

Esters of fatty acids with long-chain alcohols
Function: protective and structural functions in plants and animals

Ex. beeswax

24
Q

Nucleic Acids

A
  • RNA [cope of DNA used to make proteins] and DNA (heredity)
  • ATP (energy)
  • NAD and FAD (electron carriers)
25
Monomer of nucleic acids
Nucleotide: sugar (pentose), phosphate, nitrogenous base
26
Proteins
- make up many cell structures - numerous combinations = functional complexity - delicate, can lose funtion if denatured (extreme pH or temp. or exposure to chemicals that nravel its structure)
27
Protein Polarity
If quarternary structure has polar groups facing outwards = soluble in water If polar groups face inwards = does not dissolve in water
28
Protein Functions
1. Enzymes 2. Important structural components of living protoplasm (i.e. membranes, chromosomes) 3. Hormones (chemical messengers) 4. Plasma proteins in blood (clotting, fluid regulation buffer, antibodies 5. Transport of oxygen as hemoglobin 6. Contractile proteins in muscles 7. Extracellular proteins provide support (i.e. cartilage, bone tendons, ligaments) 8. Source of energy
29
Monomer of Proteins
Amino acids
30
Types of amino acids
20 types: - 8 essential (not made in the body) - 12 can be made in the body with the 8 essential amino acids All organisms have the same amino acids, but different organization of proteins R-group determmined the identity and unique chemical properties
31
How are proteins formed? What bond is formed?
Through a dehydration reaction Peptide bond
32
Protein Folding
4 Levels Distinguished by degree of complexity in the polypetide chain
33
Primary Level
- sequence of amino acids (chain >50) makes up a specific protein polypetide chain - determines ultimate shape or conformation - peptode linkage of amino group (NH2) one amino acid + acid group (COOH) of next amino acid
34
Secondary Level
- regular localised folding patterns of the polypeptide chain - forms alphahelix (extended outside) or beta sheets (antiparallel) - chain interacts with neighbours through H-bonding between C=O and NH2 (5 amino acid units aparts)
35
Tertiary
- local 3D shape - formed from interactions between various R-groups of amino acids - folding of the coils or sheets - hydrophilic and hydrophobic R groups - H-bonding between distant amino acids - disulphide bridges - prosthetic groups
36
Quarternary
- assembly of 2+ folded chains associating to from a functional unit - hed together by weak forces - hydrophobic interactions - H-bonding - R group interaction - Van Der Waal's forces
37
Acids
Proton Donors - soluble in watr - good conductors - litmus (turns red) - phenolphthalein (colourless) pH < 7 (low pH) Ex. organic - CH3COOH inorganic - H2SO4, HCl
38
Bases
Proton Acceptors - soluble in water - good conductors - litmus (turns blue) pH > 7 (high pH) Ex. organic - amine (NH2) inorganic - NaOH, NH3
39
Neutralization
acid + base = salt + water (incomplete) EX. NH2 + COOH-R = NH3 + COO(-)-R
40
Redox
Electron transfer reactions EX. Fe + CuSO4 = FeSO4 + Cu (e- are lost and gained)
41
Hydrolysis (hydration)
A water molecule is added EX. dipeptide + H2O = 2 amino acids
42
Dehydration/condensation
A water molecule is removed EX. esterification 3 fatty acids + glycerol = triglyceride + 3(H2O)

Biology (15 decks)

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