proteins Flashcards

(16 cards)

1
Q

proteins definition

A

complex organic substance made of carbon, hydrogen, oxygen, nitrogen
- >50% of dry mass of most cells

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2
Q

proteins are built up of…

A
  • monomers: amino acids
  • two amino acids undergo condensation reaction
    -> bond between two amino acids is strong covalent bond (peptide bond)
  • amino acids linked up by peptide bonds -> polypeptide
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3
Q

some roles of proteins

A
  • enzymatic reactions
  • structural support
  • storage
  • transport
  • cellular communication
  • movement and defense against foreign substances
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4
Q

amino acid structure

A

1) R group/side chain
- confers different chemical properties and identities of amino acids

2) amino group
- lhs (HNH)
- nitrogenous component
- basic (alkaline)

3) carboxylic acid group
- rhs
- acidic

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5
Q

amino acid categorisation (4)

A

1) non-polar neutral
2) polar neutral
3) polar acidic
4) polar basic

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6
Q

non polar neutral categorisation

A
  • non-polar: hydrophobic r group
  • neutral: no charge

methionine
- CH2, CH2, S, CH3
tryptophan
- CH2, indole ring – hydrophobic component

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7
Q

polar neutral categorisation

A
  • polar: hydrophilic R group
  • neutral: no charge

threonine
- CH, CH3, OH
tyrosine
- OH

OH groups (hydroxyl)

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8
Q

polar acidic categorisation

A
  • polar: hydrophilic R group
  • acidic: weak acid

aspartic acid
- CH2, C = O - O
glutamic acid
- CH2, CH2,C = O, O
COOH- carboxyl group

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9
Q

polar basic categorisation

A
  • polar; hydrophilic R group
  • basic: weak alkali

arginine
- CH2, CH2, CH2, NH, C =H2N, - NH2
(what group) extremely basic because its positive charge is stabilised by resonance

hisidine
C, HN, CH, HC=NH
- nitrogens have weak affinity for an H+ and are only partly positive at neutral PH

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10
Q

non-essential amino acids

A
  • can be synthesised by the body, even if not directly consumed in diet
  • body typically produces them through metabolic processes involving other amino acids or intermediates
    eg: amino acid glutamine can be synthesised from glutamate by incorporating ammonia
  • vital for physiological function
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11
Q

essential amino acids

A
  • acids ghat the human body cannot synthesise internally
  • inability due to lack of specific enzymes or metabolic pathways needed to produce these compounds
  • essential amino acids must be obtained through dietary sources (meat, diary, eggs, etc)
  • play important role in protein synthesis, tissue repair, various metabolic processes essential for growth, immune function, overall health
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12
Q

peptide bonds

A
  • linkage between amino acids and polypeptide chain
    (the amino group of one amino acid and the carboxyl group of another
  • through condensation
  • catalysed by enzymes
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13
Q

dipeptide

A

2 amino acids joined by a single bond

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14
Q

peptide

A

more than two amino acids joined by multiple peptide bonds

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15
Q

denaturation

A
  • proteins/nucleic acids lose the quaternary structure, tertiary structure and seconding structure, present in their native state
  • loss of specific #D conformation of a protein molecule
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16
Q

denaturation processes (6)

A

acids/base
organic solvents
salt solution
pressure
heat
mechanical force