Protein conformation Flashcards

1
Q

What are the structural levels of proteins structure ?

A
  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure
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2
Q

What is meant by primary structure of protein ?

A

It is type , number and sequence of AA in the polypeptide chain and it is genetically determined through the nucleotide sequence of the protein coding region of DNA , it determines secondary , tertiary and quaternary structures.

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3
Q

What stabilizes the primary structure of protein ?

A

It is stabilized by peptide bonds

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4
Q

What are the shapes of the secondary structure ?

A
  1. Alpha helix
  2. Beta pleated sheets
  3. Beta turns
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5
Q

What are the characteristics of Alpha helix ?

A
  1. It is a rod ( spiral ) structure .
  2. Side chains of amino acids extend outwards from the axis of the helix.
  3. A complete turn of the helix contain an average 3.6 aminoacyl residues.
  4. Twisting of alpha helix is right handed ( clockwise )
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6
Q

What stabilizes the alpha helix ?

A

Hydrogen bonds

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7
Q

What destabilizes the alpha helix ?

A
  1. Two adjacent R groups of the same charge ( Lys and Arg )
  2. Two adjacent bulky side chains ( Leucine and Isoleucine )
  3. Pro and Gly ( helix breakers )
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8
Q

What are the examples of the alpha helix ?

A
  1. Hemoglobin
  2. Myoglobin
  3. Alpha keratin
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9
Q

Describe the structure of the beta pleated sheets .

A

The polypeptide chains (5-10AA) are arranged in lines side by side forming beta pleated sheets.

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10
Q

Why are Beta pleated sheet called pleated ?

A

Pleated because the radical groups are arranged alternatively slightly above and below the plane of the main chain of polypeptide to form a zigzag like structure.

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11
Q

How are the beta pleated sheets stabilized ?

A

They are stabilized by the hydrogen bonds :

  1. Interchain hydrogen bonds : between separate polypeptide chains.
  2. Intrachain hydrogen bonds : between segements of the same polypeptide chain.
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12
Q

What is the role of Beta turns ?

A

Enable the polypeptide chain to reverse its direction and fold back on themselves.

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13
Q

What are the number of amino acids participating in the beta turns ?

A

4 amino acids , the first amino acid being hydrogen bonded to the fourth and it contains ( glycine , proline and hydrophilic AAs)

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14
Q

What stabilizes Beta turns ?

A

Hydrogen bonds and ionic bonds

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15
Q

What is meant by tertiary structure of proteins ?

A

Three-dimensional structure of protein. Every protein has a unique tertiary of folded secondary structure (helices , beta pleated sheets and non-regular regions ) in a specific way.

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16
Q

Why does every protein have unique tertiary structure ?

A

As the AAs of the primary structure are brought near the AAs of the secondary structure which results in interactions at different points in the secondary coiled structure forming a 3 dimensional structure that suits the function of the protein.

17
Q

What stabilizes the tertiary structure of proteins ?

A
  1. Covalent bonds : Disulphide bonds

2. Non covalent bonds : Hydrogen , Electrostatic bonds , Hydrophobic interactions.

18
Q

What is the Quaternary structure of proteins ?

A

It is the arrangement of subunits of proteins consisting of 2 or more polypeptide chains .

19
Q

What are the type of Quaternary structure ?

A
  1. Homogenous proteins : similar subunits

2. Hetrogenous proteins : different subunits

20
Q

What stabilizes Quaternary structure ?

A

Non covalent interactions

21
Q

What are the examples of Quaternary structures ?

A
  1. Creatine phosphokinase ( dimmer )

2. Hemoglobin : 4 polypeptide chains ( alpha 2 beta 2 )