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biology > B1.2 - proteins > Flashcards

B1.2 - proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

proteins

A

Complex macromolecules composed of one or more chains of amino acids

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2
Q

amino acids

A

Monomers used to make proteins

NH2 (amino group)
H (hydrogen atom attached to central carbon)
R side chain
COOH (carboxyl group)

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3
Q

bonding + reactions of amino acids in protein

A

Amino acids join together by condensation reaction
Peptide bond formed when the carboxyl group (–COOH) of one amino acid reacts with the amino group (–NH2) of another amino acid to form a dipeptide

n terminal, c terminal

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4
Q

role of proteins

A

catalysis, signalling pathways, structural support

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5
Q

word equation of amino acids to create dipeptide

A

amino acid + amino acid → dipeptide + 1 water molecule

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6
Q

essential amino acids

A

amino acids that your body CANNOT produce.
Obtain from food

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7
Q

non-essential amino acids

A

produced by body from other amino acids/ breakdown of proteins

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8
Q

genetic code

A

set of rules specifies how info in DNA is translated into sequence of amino acids

universal language of all living things

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9
Q

transcription

A

DNA —> mRNA

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10
Q

translation

A

mRNA —-> sequence of amino acids

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11
Q

codon

A

group of 3 nucleotides that specify type of amino acid/ stop signal required

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12
Q

genetic code is degenerate

A

multiple codons (64) can code for the same amino acid (20)

allows for silent mutations!!

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13
Q

peptide bond

A

covalent/stable bond between carboxyl group of one amino acid to amino group of the other amino acid

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14
Q

lets add another amino acid to the chain

A

n-terminal NOT involved in peptide bonds, new amino acids are added to the c-terminal

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15
Q

list examples of polypeptides

A

lysozyme, alpha-neurotoxins, glucagon, myoglobin

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16
Q

lysozymes

A

enzyme composed of 129 amino acids

tears and saliva

antimicrobial properties (disrupts cell wall)

17
Q

How do extremes of pH impact the structure of a protein?

A

It denatures the protein by changing the 3D conformation

18
Q

haemoglobin

A
  • 4 polypeptide chains
  • conjugated protein
  • binds to oxygen
  • 4 subunits held by h-bonds
19
Q

denaturation of protein (2 factors)

A

pH and temp (breaks weak h-bonds)

20
Q

conjugated protein
(definition + example)

A

contains non-protein components (metal ions, carbohydrates)

ex. haemoglobin

21
Q

non-conjugated proteins

A

contains only polypeptide subunits

ex. insulin, collagen

22
Q

alpha-neurotoxins

A

polypeptide

  • 60-75 amino acids
  • snake venom
  • targets nervous system
23
Q

glucagon

A

polypeptide
- hormone

  • 29 amino acid residues
  • regulates blood sugar lvls
  • secreted from pancreas
24
Q

myoglobin

A

polypeptide
- oxygen binding protein

  • 153 amino acids
  • muscle tissues
  • storage and release of oxygen to muscle fibres (used in physical activity)
25
Q

R-groups (properties)

A
  • hydrophobic/ hydrophilic
  • hydrophobic are non-polar, repels water
  • hydrophilic are polar, contains partial charges
    basic (+)
    acidic (-)
26
Q

primary structure of proteins

A

refers to specific sequence of amino acids joined together to form polypeptide chains
- determines how the chain will fold (3D shape!)

27
Q

secondary structure of proteins

A

refers to local folding patterns that occur within the polypeptide chain
- alpha helices
- beta-pleated sheets

28
Q

alpha helices

A
  • hydrogen bonds form between amine hydrogen of one amino acid and carboxyl oxygen of another amino acid 4 residues away in the sequence
  • allows coiling
29
Q

beta-pleated sheets

A
  • sections of the polypeptide run parallel
  • h-bonds form between adjacent strands
30
Q

tertiary structure of proteins

A

further folding
(interactions + bonding between R groups)

H-bonds, ionic bonds, disulfide covalent bonds, hydrophobic interactions

31
Q

hydrogen bonding (tertiary)

A
  • between polar R groups
  • stabilizes 3D shape (holds distant regions tgt)
32
Q

ionic bonding (tertiary)

A
  • R groups go through binding & dissociation of H+ ions to create charged R groups
33
Q

disulfide covalent bonds (tertiary)

A
  • forms between pairs of cysteine (contains sulfur)
34
Q

hydrophobic interactions (tertiary)

A
  • occur between non polar amino acids
  • cannot interact with water, so they clump tgt in clusters in the inside of proteins
35
Q

globular proteins (+ example)

A
  • spherical, irregular folds
  • soluble
  • enzymes, transporters, regulators

ex. insulin, myoglobin

36
Q

fibrous proteins (+ example)

A
  • long, narrow
  • stability for skin, tendons, bone

ex. collagen

37
Q

quaternary structure of proteins

A
  • arrangement/ interaction of 2 or more polypeptide chains
38
Q

insulin

A
  • hormone regulating amount of glucose in the body
  • produced by pancreas
  • binds to receptors of the cell, allowing glucose to enter)
  • compact and GLOBULAR
  • hydrophobic exterior, hydrophilic interior
39
Q

collagen

A
  • most abundant protein in the body (forms connective tissues + skin, cartilage)
  • made of 3 polypeptide chains twisted in a triple helix
  • fibrous protein
  • contains glycine and proline residues

biology (8 decks)

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