1.6 proteins Flashcards

1
Q

What is the size, shape and frequency of proteins?

A
  • Proteins are very large molecules
  • Each organism has numerous proteins which are unique to their species
  • the shape of any one protein molecules differs from every other type of protein, and is very specific to its function.
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2
Q

What are amino acids?

A

the basic monomer that make up the polypeptide polymer, which make up proteins.

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3
Q

What is the structure of an amino acid?

A

Each amino acid has a central carbon atom with four different chemical groups attached:
1) AMINO GROUP: (-NH2)- a basic group
2) CARBOXYL GROUP: (-COOH)- an acidic group
3) HYDROGEN
4) R GROUP: a variety of different chemical groups.
each amino acid has a different R group

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4
Q

Describe the formation of a dipeptide.

A

Two amino acids undergo a conensation reaction which causes the formation of a peptide bond between the carbon of one AA and the nitrogen atom of the other.

  • the water molecule is made from combining the -OH of the carboxyl group and the -H from the amino group of another amino acid.
  • likewise, the molecule can be broken up by the adition of water (hydrolysis)
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5
Q

What is a polypeptide and how is it formed?

A

A chain of hundreds of amino acids formed by a series of condensation reactions.

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6
Q

What is the primary structure of a protein?

A

The sequence of amino acids in a polypeptide.

  • sequence is determined by DNA
  • Determines protein’s ultimate shape and therefore function.
  • a change in a single amino acid will change or stop the function.
  • Simple proteins may only ave one, but most proteins have multiple polypeptide chains.
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7
Q

Describe the secondary structure of a protein.

A
  • The amino acid chains which make up a polypeptide possess -NH and -C=O groups on either side of the peptide bond.
  • The -NH group has a + charge and the O of the -C=O group has a - charge.
  • this means they readily form weak hydrogen bonds this causes the polypeptide chain to be folded into a 3D shape such as an alpha helix coil.
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8
Q

Describe the tertiary structure of a protein.

A
  • The secondary structures of a protein can be twisted and folded further into a complex and specific 3D shape, known as the tertiary structure.
  • these are maintained by a number of different bonds
  • the tertiary structure makes each protein distinctive and makes it recognizable.
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9
Q

What are the bonds which make up the tertiary structure of a protein?

A

DISULFIDE BRIDGES: fairly strong, not easily broken
IONIC BONDS: formed between a carboxyl and amino groups not involved in forming peptide bonds. weaker and easily broken by changes in PH
HYDROGEN BONDS: numerous but easily broken.

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10
Q

describe the quaternary structure of a protein.

A

Large proteins form complex molecules containing a number of polypeptide chains linked in various ways.
- may also include non-protein groups, eg: iron in the haem group if haemoglobin

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11
Q

What is the test for protiens?

A

Biuret test to detect peptide bonds:

1) Place sample in a test tube and add an equal volume of sodium hydroxide at room temp.
2) Add a few drops of very dilute copper (II) sulfate solution and mix gently
3) A purple colouration indicates the presence of of peptide bonds. if solution stays blue, no protein is present.

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