Macromolecules and Proteins Flashcards

1
Q

what are the 4 major families of small organic molecules and the subunits and macromolecules

A

sugars -> polysaccharides
fatty acids -> fats/lipids/membranes
amino acids -> proteins
nucleotides -> nucleic acids

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2
Q

what reaction forms macromolecules

A

condensation = covalent bond through loss of water
hydrolysis (reverse) = break apart with water

require ATP and catalyst

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3
Q

what is the simplest sugar

A

monosaccharides
- have 6 carbon ring

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4
Q

types of sugars and uses

A

starch = storage
cellulose = building material

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5
Q

What is the one group that does not form polymers

A

Lipids
Grouped because they are insoluble in water (soluble in fats/oil)

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6
Q

Structure of fatty acids

A

Long hydrocarbon chain (hydrophobic)

Carboxyl group (-COOH) (hydrophilic)

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7
Q

Structure of glycerol

A

Alcohol
3 Carbons each with hydroxyl group (-OH)

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8
Q

Structure of Phospholipids

A

Glycerol with
- 2 fatty acids (hydrophobic tail)
- 3rd hydroxyl group joined to phosphate group (hydrophilic head)

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9
Q

How do glycerol and fatty acids bond

A

Form covalent bond though dehydration reaction with hydroxyl group

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10
Q

Types of proteins

A
  • enzyme - catalyse reactions
  • gene regulation - switch on/off
  • structure
  • transport - though membranes, around body (haemoglobin)
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11
Q

How do membranes form

A

Double layer of phospholipids arrange themselves with the hydrophobic tails on the interior and the hydrophilic heads on the outside to aqueous environments to minimise free energy

= phospholipid bilayer

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12
Q

Structure of Amino Acid

A

C
H
- Carboxyl group (-COOH)
- Amino group (NH2)
- R group

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13
Q

What type of bond forms between AA in creating proteins

A

Peptide bonds
Link C1 to N2

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14
Q

What is the primary protein structure

A

Specific sequence of AA that make up the protein chain

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15
Q

What is the secondary protein structure

A

Hydrogen bonds between H and O in amino and carboxyl groups twist chains into coils or sheets

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16
Q

What is the protein tertiary structure

A

R groups interact by
- ionic bonds
- disulphide bridge
- H bonds
- hydro interactions
to create 3D shape depends on AAs

17
Q

What is protein quaternary structure

A

Multiple polypeptide chains associate to form a functional protein

18
Q

How can mutations / substitutions in amino acids impact protein function

A
  • if mutation in codon, most likely will still encode for same AA anyway due to redundancy
  • If different AA may result in very different overall shape and therefore function
  • Sickle cell example