2.1.2 M) Levels of Protein Structure Flashcards

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1
Q

Primary protein structure:

A

sequence of amino acids bonded by covalent peptide bonds

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2
Q

How is the primary structure of a protein formed?

A
  • condensation reacts bonds amino acids together and water molecule(s) is released
  • covalent peptide bond between the amino acids
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3
Q

What is the primary structure specific for?

A

the primary structure us specific for each protein (one alteration in the sequence of amino acids can affect the function of the protein)

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4
Q

What is the secondary protein structure?

A
  • initial folding of the protein
  • weak negatively charged nitrogen and oxygen atoms interact with weak positively charger hydrogen atoms to form hydrogen bonds which holds the initial folding in place
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5
Q

What shapes are formed in the secondary structure?

A
  • α-helixshape
  • β-pleated sheetshape
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6
Q

Which proteins have a secondary structure?

A

most fibrous proteins e.g. collagen and keratin

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7
Q

How can the bonds in the secondary structure be broken?

A

the hydrogen bonds can be broken by high temperatures and pH changes

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8
Q

Diagram of α-helixshape and β-pleated sheetshape

A
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9
Q

Tertiary protein structure:

A
  • 3D shape formed and held together by 4 bonds
  • bonds formed between R groups of amino acids
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10
Q

What bonds are formed in the tertiary protein structure?

A
  • Hydrogen- between strongly polar R groups
  • Disulphide bond/bridge- only occurs between 2 sulphurs on 2 R groups (only 3 types of amino acids contain sulphur so bond is rare)
  • Ionic - between charged R groups
  • Hydrophobic/philic interactions- between non-polar R groups within the interior of proteins
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11
Q

What proteins is the tertiary structure common in?

A

common in globular proteins

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12
Q

Order of weakest to strongest bonds in tertiary structure:

A
  • H bond
  • ionic bond
  • disulphide bond/bridge
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13
Q

What does tertiary structure determine?

A
  • A polypeptide chain will fold differently due to the interactions (and hence the bonds that form) betweenR groups
  • Each of thetwenty amino acidsthat make up proteins has a uniqueR groupand therefore many different interactions can occur creating a vast range of protein configurations and therefore functions
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14
Q

How can a change in the amino acid sequence result in the formation of a non-functional enzyme?

A
  • change in aa sequence
  • leads to change in primary structure
  • so dif. order of R groups
  • dif. secondary structure - may change hydrogen bonding → H bonds may not form or form in different places
  • dif. tertiary structure - R groups in dif. places so tertiary bonds may form differently
  • 3D shape is different
  • so active site no long complementary to substrate
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15
Q

How is a proteins tertiary structure disrupted when heated to a high temp?

A
  • increase in kinetic E of protein
  • protein vibrates/moves more
  • hydrophobic/philic / hydrogen / ionic bonds / interactions break
  • change in 3D shape/conformation of protein
  • denatures enzyme
  • active site changes shape and is no longer complementary to substrate
  • enzyme stops working
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16
Q

What proteins have a tertiary structure?

A

most enzymes

17
Q

Quaternary protein structure:

A
  • multiple tertiary structures/polypeptide chains joining together
  • same 4 bonds as tertiary structure
18
Q

What is each polypeptide chain in the quaternary structure of a protein referred to as?

A

referred to as asubunitof the protein