topic 1.3 - proteins Flashcards

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1
Q

primary structure of a protein

A

sequence of an amino acids that make up the polypeptide chain

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2
Q

secondary structure

A

can either be alpha helix or beta pleated sheet

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3
Q

what is the sequence of a protein determined by

A

the DNA of the gene that encodes the protein. Even changing just one amino acid in a protein’s sequence can affect the proteins overall structure and function

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4
Q

importance of insulin and glucagon as proteins

A

control blood glucose concentration

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5
Q

how is an α-helix formed

A

due to hydrogen bonds forming between the oxygen of -CO group of one amino acid and the hydrogen of the -NH group of the amino acid 4 places ahead of it

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6
Q

how is a β-pleated sheet formed

A

two or more segments of a polypeptide chain line up next to each other forming a sheet like structure held together by hydrogen bonds

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7
Q

tertiary structure

A

folding of the protein in order to form a precise 3D shape

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8
Q

bonding in a tertiary structure

A
  • hydrogen bonds : formed between polar groups like -NH, -CH, -OH groups (broken & reform by change in temp or pH)
  • disulfide bonds : formed between two cysteine molecules which are close in strcuture of a polypeptide. Much stronger than hydrogen bonds as it is covalent. (broken by reducing agents)
  • ionic bonds : between ionised amine (NH3+) and ionised carboxylic acid (COO-)
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9
Q

quarternary structure

A

proteins are made up of two or more polypeptide chains

held together by hydrogen bonds, disulphide bonds & ionic bonds

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10
Q

globular proteins

A
  • proteins that curl up into a ball shape so their hydrophobic groups are in the centre while the hydrophilic groups remain on the outside and relate well to the blood
    • enzymes
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11
Q

fibrous proteins

A
  • molecules do not curl up
    • not soluble in water
    • role is mostly structural
    • e.g. collagen, keratin
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12
Q

globular protein - haemoglobin

A
  • carries oxygen and found in red cells
  • 4 polypeptide chains
  • each polypeptide chain is called a Globin held together by disulfide bonds
  • each chain is arranged around a haem group (contains iron)
  • iron enables haemoglobin to bind to and release oxygen molecules
  • when haemoglobin binds to oxygen it is bright red, when there is no oxygen it is blue/purple
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13
Q

fibrous protein - collagen

A
  • most common protein found in animals
  • not folded; form strands
  • insoluble as it provides a structural function
  • 3 polypeptide chains arranged in a triple helix held together by hydrogen and covalent bonds
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14
Q

advantages of collagen

A
  • flexible
  • high tensile strength so not easy to break when pulled
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