protein Flashcards

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1
Q

what is proteins made up of

A

carbon, hydrogen, oxygen, nitrogen

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2
Q

what are the functions

A
  • enzymes to catalyse reactions
  • carrier proteins transport molecules across membranes
  • antibodies defend against diseases
  • structural proteins support cells and tissues
  • hormones transmit information
  • transport proteins (haemoglobin) carry oxygen
  • contractile proteins enable muscles to contract
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3
Q

why do diffrent proteins carry out different functions

A

have different shapes

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4
Q

what are make up proteins

A

amino acid polymer

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5
Q

what 4 molecules are in an amino acid

A

-carboxylic acid group
- amine group
- hydrogen
- R- one of 20 different groups

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6
Q

how many essensial amino acids are there

A

8
- cant be synthesised by the body

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7
Q

what reaction joins amino acids

A

condensation reaction
- removes wtare molecule and forms a peptide bond between the amino group and carboxylic group of the other amino acid

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8
Q

how is a polypeptide chain formed

A

the amino end and the carboxylic end of a dipeptide react with another amino acid

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9
Q

what are the levels of protein structure

A
  • primary
  • secondary
  • teritary
  • quaternary
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10
Q

what is the primary structure

A

the sequence of amino acids is held togtehre by peptide bonds (polypeptide)

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11
Q

what is the secondary structure

A

folding of the primary structure

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12
Q

types of secondary structure

A

alpha helix- when polypeptide chain coils
beta pleated sheet- folds

both held togteher by weak carbon bonds

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13
Q

examples of secondary structure

A

keratin- functional protein

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14
Q

what is the tertiary structure

A

further folding of the polypeptide chain to give more compex 3D shape

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15
Q

what is found in both teriary and quaternary structure

A
  • hydrogen bonds between polar R groups
  • disulphide bonds- covalent bonds formed between sulphurs in the R group of amino acid cystiene
  • ionic bonds between positively and negatively cahrges R groups
  • hydrophobic interactions- between non-polar R groups which cluster together towards centre of molecule
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16
Q

what is the quaternary stucture

A

made of more than one polypeptide chain

17
Q

example of quaternary structure

A

haemoglobin

18
Q

how do proteins denature

A

heating increases the kinetic energy causing atoms to vibrate and weak bonds to break
this can lead to the whole tertiary structure unraveling and the protein will be permanently denatured

19
Q

types of proteins

A

globular, fibrous

20
Q

properties of fibrous
proteins

A
  • from fibres
  • insoluble in water
  • have structural roles found in skin, tendons, bones, cartilage
  • doesnt contain a prosthetic group
21
Q

properties of globular
proteins

A
  • rolls up to form balls
  • soluble in water
  • metabolic role- carries oxygen in red blood cells
  • contains a prosthetic group- haem
22
Q

properties of haemoglobin

A
  • 4 folded polypeptide chains
  • 4 iron conatining haem group
  • compact and spherical
  • soluble in water
23
Q

why is collagen strong

A

the collagen molecules cross link through covalent bonds to form fibres which give collagen its strength

24
Q

properties of collagen

A
  • made from 3 identical left handed helix polypeptide cahins wound to make a triple helix
  • in each cahin, the third amino acid is glycine
  • chains held together by hydrogen bonds
  • very stable/insoluble in water