1.6 Proteins Flashcards

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1
Q

What are proteins made up of

A

Amino acids

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2
Q

Describe the structure of an amino acid (like the groups in the amino acid)

A

*Amine group (NH2) on the left
* Carboxyl group on the right (C=OOH)
* R group/ variable group at the top
and a C and a H below the carbon

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3
Q

Describe how amino acids are joined together to form a dipeptide

A
  • Condensation reaction
  • Water is removed
  • Peptide bond forms between OH of carboxyl and H of the Amine group
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4
Q

What is the name of the bond between the amine group and the carboxyl group

A

Peptide bond

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5
Q

What are proteins

A

Polymers made up of the monomer amino acids

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6
Q

What are the 4 different level of structure in a protein

A

Primary
Seconday
Teritiary
Quarternary

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7
Q

What is the primary structure is

A

The sequence of amino acids in a polypeptide chain

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8
Q

What is the secondary structure

A
  • Folding (repeating patterns) of polypeptide chains e.g. alpha helix or beta pleated sheets
  • Due to hydrogen bonds between amino acids
  • between the NH and C=O
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9
Q

What are the secondary structures held together by

A

Hydrogen bonds hold them together

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10
Q

Where do the Hydrogen Bonds form in the secondary structure

A

Between the C=O group of the Carboxyl group of one amino acid and the H in the Amine group of another amino acid

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11
Q

What is the tertiary structure

A

*Protein gets further foldings of the secondary structure
*Forming a unique 3D shape
*Held in place by Ionic, Hydrogen and disulphide bonds

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12
Q

Where do the ionic and Disuphide bonds form in the tertiary structure

A

Between the R groups of different amino acids

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13
Q

When do you get disulphide bonds

A

If both amino acids have sulphur in their R groups

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14
Q

Describe the quaternary structure of a protein

A

More than one polypeptide chain
Formed by interactions between polypeptides (hydrogen bonds ionic bonds and disulfide bridges)

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15
Q

What is an example of a quarternary structure protein

A

Haemoglobin

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16
Q

What happens if a protein denatures

A

The bonds which hold the tertiary structure and secondary structure break and therefore their unique shape is lost

17
Q

What are the conditions that cause enzymes to denature

A

Too high a pH( too many H+ions or OH- ions)
Too high a temperature (too much kinetic energy)

18
Q

What is the importance of the primary structure

A

If even one amino acid in the sequence changes it will cause the Ionic, Hydrogen or disulphide bond to form at a diff location resulting in a diff 3D shape

19
Q

What is an example of different 3D shapes (in carrier proteins)

A

They will have a different shaped binding site

20
Q

What are dipeptides and polypeptides

A

Dipeptides- 2 amino acids joined together
Polypeptide- Many amino acids joined together

21
Q

How many amino acids are common in all organisms and how do they vary

A

20 amino acids and they vary in thier R group