Protein Structure Levels Flashcards

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1
Q

How many different levels can proteins take?

A

4 different levels

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2
Q

What are the 4 different levels of protein structure?

A

Primary, Secondary, Tertiary and Quarternary

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3
Q

Describe a primary protein structure

A

Linear sequence of amino acids

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4
Q

What are the 3 secondary structures for proteins?

A
  • α - helix
  • β - pleated sheet
  • Random coil
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5
Q

Describe α - helix secondary protein structure

A
  • Spiral shaped amino acid chain fortified by weak hydrogen bonds
  • Elastic in nature (can be stretched). returns to original shape after being stretched.
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6
Q

Describe β - pleated sheet secondary protein structure

A
  • Triangular patterned amino acid chain fortified by weak hydrogen bonds.
  • Represented through directional arrows.
  • Cannot be stretched (already fully extended)
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7
Q

Describe Random coil secondary protein structure

A
  • Irregular shaped amino acid chain fortified by weak hydrogen bonds.
  • It is most active region of molecule.
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8
Q

Describe structure of tertiary proteins

A

Tertiary proteins have a unique shape consisting of primary and secondary amino acid chain sections

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9
Q

Describe Structure of Quarternary Proteins

A

Multiple chains of amino acids (tertiary groups) joining together to form a larger unique shaped protein

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10
Q

Which structure levels are non-functional (unpurposeful)

A

Primary and Secondary structure levels

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11
Q

Which structure levels are functional (purposeful)

A

Tertiary and Quarternary structure levels

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12
Q

What are the 4 types of bonds/interactions found in tertiary and quarternary structures?

A
  • Hydrogen Bonds
  • Ionic Bonds
  • Disulphide bridges
  • Interactions between hydrophobic and hydrophilic R groups
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13
Q

What is the purpose of these bonds found within tertiary and quaternary structures?

A

To help the protein maintain it’s structure and give the shape stability

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14
Q

What is a prosthetic group?

A

A group that is part of a protein but is not made of amino acids

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15
Q

What is the importance of protein’s having a unique shape?

A

Each protein can fulfill it’s purpose due to it’s unqiue shape

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16
Q

How does a DNA mutation affect the creation of a protein?

A

Creates a non-functional protein

17
Q

What determines the shape and folding of proteins?

A

The properties of the functional groups found on the amino acids

18
Q

Which amino acids generally face inside and outside

A

Hydrophobic amino acids face inwards while hydrophilic amino acids face outwards

19
Q

Which amino acids like to come closer towards each other during the folding process of proteins?

A

Hydrophobic proteins like to come towards each other. Acidic and Basic amino acids that hold polar charges also attract each other.

20
Q

A prosthetic group forms what type of protein?

A

Conjugated Protein

21
Q

What are peptides?

A

Linear sequences of amino acids shorter than 50 amino acids.