Proteins Flashcards

1
Q

list all 8 protein functions:

A
  • enzymes
  • defence
  • storage
  • transport
  • hormonal
  • receptor
  • movement
  • structural
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2
Q

how much dry mass do proteins account for:

A

50%

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3
Q

enzymes:

A
  • accelerate chemical reactions

- lock and key mechanism

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4
Q

defensive:

A

eg. antibodies help inactivate and destroy bacteria and viruses
- recognise pathogens and target them

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5
Q

storage:

A
  • store amino acids
  • eg. casein protein of milk is major source of amino acids for baby mammals
  • ovalbumin protein for egg white, amino acid source for developing embryo
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6
Q

transport:

A

transport substance

  • haemoglobin: iron-containing protein
  • carries molecules
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7
Q

hormonal:

A
  • allows different components (organs or tissues) of an organism to communicate
    eg. insulin, causes other tissues to take in glucose, to regulate blood sugar levels
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8
Q

receptor:

A

signals response to stimuli

- receptors in nerve cell detecting molecules

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9
Q

movement:

A

flagella, cilia and muscle

  • proteins actin and myosin responsible for contraction of muscles
  • motor proteins for cilia and flagella responsible for contraction of muscles
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10
Q

structural:

A
  • support
  • keratin protein in hair, skin, feathers
  • collagen and elastin proteins provide framework in animal connective tissues
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11
Q

polypeptides:

A

polymers built from 20 amino acids (charged, hydrophobic, hydrophilic)

  • unique linear sequence of amino acids
  • proteins have one or more polypeptides
  • 10 to 1000 amino acids in length
  • amino acids linked by peptide bonds
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12
Q

amino acids:

A

organic molecules, carboxyl and amino groups

- amino acids differ in properties due to R groups (side chains)

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13
Q

peptide bonds:

A

to join amino acids together

- carboxyl (COOH) and amino (NH2( groups form peptide bonds, loses water in process

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14
Q

functional protein consists of:

A

1 or more polypeptides twisted and folded into 3D structure

- sequence of amino acids determines structure of protein

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15
Q

structure of protein determines? and what else affects function

A

its function,

  • only some amino acids are exposed on surface of protein,
  • physical and chemical properties of these also affect function
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16
Q

types of structural models

A
  • space filling
  • ribbon
  • wire frame
17
Q

primary structure:

A

unique sequence of amino acids

- determined by DNA

18
Q

secondary structure:

A

coils and folds from hydrogen bonds btw amino acids in polypeptide

  • alpha helix (coil)
  • beta pleated sheet (fold)
19
Q

list 4 chemical bonds:

A
  • hydrogen bonds
  • van der Waals interactions
  • ionic bonds
  • disulphide bonds
20
Q

hydrogen bonds:

A

H atom + electronegative atom (eg. O or N)

21
Q

van der Waals interactions:

A

uneven distrubution of electrons, dynamic positive/negative charge, allows weak bonding btw molecules

22
Q

ionic bonds:

A

btw cation (positive) and anion (negative)

23
Q

disulphide bonds:

A

covalent bond btw two sulphur atoms

24
Q

tertiary structure:

A

interactions btw R groups

  • H bonds, ionic, hydrophobic, van der Waals interactions
  • strong disulphide bridges may reinforce protein structure
25
Q

quaternary structure:

A

two or more polypeptide chains forming one macromolecule

26
Q

chaperones:

A
chaperone proteins (chaperonins) aid in correct folding of protein
- cap and hollow cylinder provide safe space for proper folding
27
Q

protein structure: other conditions

A

physical and chemical can also affect protein structure
- pH
- salt conc.
- temperature
- environment
causes protein to unfold
- loss of native protein structure cause denaturation
- denatured protein in biologically inactive

28
Q

eg. of denaturation

A

protein thermal denaturation (irreversible) egg white cooking, albumen denatures - cross links

29
Q

eg. sickle cell haemoglobin

A

normal structure: proteins don’t associate with one another and carries O2 full capacity

vs sickle cell:
- proteins combine into fibre, greatly reducing oxygen carrying capabilities

30
Q

eg. diseases from irregular protein folding

A
  • Alzheimers
  • Parkinson’s
  • Huntington’s