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Biological Molecules > Proteins > Flashcards

Proteins Flashcards

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Organic Chemistry 101 flashcards
1
Q

monomer?

A

amino acids

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2
Q

chemicals?

A

C, H, O, N

some have sulfur

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3
Q

amino acid structure

A

look at notes

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4
Q

How is a dipeptide formed?

A

2 amino acids join together by a peptide bond in a condensation reaction where water is released

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5
Q

What happens in a hydrolysis reaction?

A

water is used to break the peptide bonds so a dipeptide breaks into amino acids

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6
Q

What is a protein made of?

A

proteins are made of 1 or more polypeptides

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7
Q

primary structure of proteins

A
  • sequence of amino acids in a polypeptide chain
  • peptide bonds only
  • a change in one amino acid may change the structure of the whole protein
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8
Q

secondary structure of proteins

A
  • hydrogen bonds form between nearby amino acids in chain making it automatically coil into an alpha-helix or fold into a beta-pleated sheet
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9
Q

tertiary structure of proteins

A
  • further folding or coiling of chain
  • more bonds form between different parts of the polypeptide chain
  • it forms the final 3D structure for proteins with a single polypeptide chain
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10
Q

What is the tertiary structure responsible for?

A
  • the shape of the active site in enzymes

- the shape of channels in channel proteins

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11
Q

quarternary structure of proteins

A
  • the way 2 or more polypeptide chains are assembled together
  • the cross-linking of 2 or more polypeptide chains
  • forms the final 3D structure for proteins with more than 1 polypeptide chain
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12
Q

bonds in primary structure

A

peptide bonds only

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13
Q

bonds in secondary structure

A

peptide and hydrogen bonds

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14
Q

bonds in tertiary structure

A
  • ionic bonds
  • disulfide bonds
  • hydrophobic + hydrophilic interactions
  • Hydrogen bonds
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15
Q

Ionic bonds

A

attractions between negatively charged R groups and positively charged R groups.

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16
Q

Disulfide bonds

A

when 2 molecules of amino acid cysteine come close together, the sulphur atom in one cysteine bonds to the sulphur atom in another cysteine forming a disulfide bond

17
Q

Hydrophobic and hydrophilic interactions

A

when hydrophobic R groups come close together in protein, they clump together. Hydrophilic R groups are more likely to be pushed to the outside affecting how the protein folds up in its final structure.

18
Q

Hydrogen bonds

A

weak bonds between slightly positively charged hydrogen atoms in some R groups and slightly negative charged atoms in other R groups on the polypeptide chain

19
Q

bonds in quarternary structure

A
  • determined by tertiary structure of individual polypeptide chains being bonded together which allows it to be influenced by all bonds
20
Q

globular proteins properties

A
  • ball shaped
  • hydrophilic R groups pushed outwards forming Hydrogen bonds with water causing hydrophobic and hydrophilic interactions making it soluble so easily transported in fluids
21
Q

Examples of globular proteins

A
  • haemoglobin
  • insulin
  • amylase
22
Q

Haemoglobin

A
  • carries oxygen around the body in red blood cells
  • conjugated protein (protein with a non-protein group attached)
  • each of the 4 polypeptide chains have a prosthetic group called Haem
  • Haem contains iron which oxygen bind sto
23
Q

Insulin

A
  • hormone secreted by pancreas
  • regulated blood glucose levels
  • soluble so transports to the tissues where it acts via blood
  • consists of 2 polypeptide chains held together by disulfide bonds
24
Q

amylase

A
  • enzyme that catalyses the breakdown of starch in digestive system
  • made of a single chain of amino acids
  • secondary structure has both alpha helix and beta pleated sections
25
Q

Fibrous proteins properties

A
  • insoluble
  • long strands (rope-like fibres)
  • strong
  • fairly unreactive
  • structural proteins
26
Q

Examples of fibrous proteins

A
  • collagen
  • keratin
  • elastin
27
Q

Collagen

A
  • in animal connective tissue (bone, skin, muscle)
  • very strong molecule
  • minerals bind to protein to increase its rigidity
28
Q

Keratin

A
  • in external structures of animals (skin, hair, nails, horns, feathers)
  • flexible - in skin
  • hard and rough - in nails
29
Q

Elastin

A
  • in elastic connective tissue (skin, large blood vessels, ligaments)
  • elastic so allows tissues to return to their original shape after stretching
30
Q

What is a conjugated protein?

A
  • a protein with a non-protein group attached
  • non-protein group is called a prosthetic group
  • example is haemoglobin

Biological Molecules (7 decks)

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