Protein structure Flashcards

1
Q

proteins

A

polymers made of monomers called amino acids

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2
Q

monomers of polypeptides

A

monomers

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3
Q

how many amino acids are there

A

20

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4
Q

structure of amino acid

A

Central carbon atom bonded to:
- Amine
- carboxylic group
- hydrogen atom
- R group

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5
Q

bonds formed between amino acids

A

peptide bonds

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6
Q

peptide bonds

A
  • covalent bonds
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7
Q

how do peptide bonds form

A

An -OH is lost from the carboxylic group of one amino acid and an H atom is lost from the amine group of another via condensation reaction

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8
Q

dipeptides

A

formed by the condensation of two amino acids

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9
Q

polypeptides

A

formed by the condensation of many amino acids

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10
Q

what happens during a hydrolysis reaction

A

peptide bond breaks with the addition of water, breaking it down to amino acids

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11
Q

primary structure

A
  • sequence of amino acids in a polypeptide chain
  • bonding: peptide bond
  • determins proteins overall shape and function
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12
Q

secondary structure

A
  • folding or coiling of the polypeptide chain into a- helixs or beta pleated sheets
  • hydrogen bonds between -C=O group of one amino acid and the amine group of another
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13
Q

what does secondary structure forms

A

a-helix: coiled structure stabalized by hydrogen bonds
B- pleated: Zig zag pattern forming sheat-like structures

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14
Q

tertiary structure- definition

A

three-dimensional folding of a polypeptide, giving the protein its functional shape

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15
Q

tertiary structure bonding

A
  1. H bonds: weak between polar groups
  2. ionic bonds: oppositely charged R- groups
  3. Disulfide bonds: covalent between sulfur attoms
  4. Hydrophobic interactions: Nonpolar R groups clustering away from water
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16
Q

quaternary structure definition

A

arrangement of 2 or more polypeptide chains into functional protein

17
Q

examples of quaternary structures

A

haemoglobin
collagen

18
Q

haemoglobin

A

water-soluble globular protein

19
Q

collagen

A

fibrous protein consisting of 3 polypeptide chains wound around each other

20
Q

globular proteins

A

compact
roughly spherical

21
Q

why do globular proteins form spherical shape when folding into their tertiary structure

A
  • non polar R groups are oriented towards the centre of the protein, away from aqueous surroundings
  • polar hydrophillic R groups oriente themselves towards the outside
22
Q

globular proteins functions

A

physiological roles as they are easily transported around and are involved in metabolic reactions

23
Q

haemoglobin structure

A
  1. polypeptide chains
    - two alpha chains
    - two beta chains
  2. haem group
    - 4 haem groups, that contain Fe2+ that binds to oxygen
24
Q

collagen structure

A
  • 3 polypeptide chains closely held together by hydrogen bonds to form a triple helix
  • each of the 3 chains are coils
  • hydrogen bonds form between the coils
  • covalent bonds form cross-links between R groups of amino acids, in interacting triple helices
25
Q

collagen function

A
  • form structure of bones
  • makes up cartilage and connective tissue
  • prevents blood from bursting walls of arteries
  • the main component of tendons