3. 1. 4. 1 Properties of Proteins Flashcards

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1
Q

What are amino acids?

A

Amino acids are the monomers from which proteins are made.

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2
Q

What are the different groups in the genrral structure of an amino acid?

A
  • Amine group (NH2) basic
  • Carboxyl group (COOH) acidic
  • Side chain (R)
  • Hydrogen atom
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3
Q

What do the 20 amino acids that are common in all organisms differ by?

A

Their side group

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4
Q

What does a condensation reaction between two amino acids form?

A

A peptide bond

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5
Q

How is a dipeptide formed?

A

By the condensation of two amino acids. The two amino acids become linked by a new peptide bond between the carbon atom of one amino acid and the nitrogen atom of the other.

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6
Q

How are polypeptides formed

A

By the condensation of many amino acids

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7
Q

What may a functional protein contain?

A

One or more polypeptide

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8
Q

What is the role of ionic bonds in the structure of proteins?

A

Tertiary structure: More bonds form between different parts of the polypeptide chain, including hydrogen and ionic bonds in the further coiling or folding of the chain.

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9
Q

What is the role of disulfide bridges in the structure of proteins?

A

Disulfide bridges form whenever two molecules of the amino acids cysteine come close together - the sulfur atom in one cysteine bonds to the sulfur atom in the other.

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10
Q

What is the primary structure of a protein?

A

Chain of amino acids joined by polymerisation. Lots of condensation reactions and peptide bonds. Known as polypeptide chain.

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11
Q

What does the primary structure determine?

A

Determines properties of protein through type and sequence of amino acids. Controlled by DNA (protein synthesis).

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12
Q

What is the secondary structure of a protein?

A

Secondary structure: Hydrogen bonds form between the amino acids in the polypeptide chain, causing it to be twisted into a 3D shape such as a coil (alpha helix) or fold (beta pleated sheet).

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13
Q

What is the tertiary structure of a protein?

A

Further bending or folding of secondary structure forming a 3D globular shape - shape is precise and specific to the function fo the polypeptide.

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14
Q

What is the quaternary structure of a protein?

A

Folding together more than one polypeptide chain.

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15
Q

What does the ‘R’ group of an amino acid determine?

A

How it bends and what bonds are formed. There are 3 types of side chain interactions:
- Hydrogen bonds
- Disulfide bonds
- Ionic bonds

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16
Q

Describe the biuret test for proteins.

A

1) Add food sample to test tube.
2) Add 2ml NaOH and 5-6 drops of CuSO4 solution.
3) Shake gently
4) Allow mixture to stand for 4-5 minutes.
5) Bluiesh/violet colour indicates presence of protien.

17
Q

What are the 4 different types of amino acids?

A
  • Nonpolar (hydrophobic) with hydrocarbon side chains
  • Polar (hydrophilic) with polar or ionic side chains
  • Acidic (hydrophilic) with acidic side chains
  • Basic (hydrophilic) with NH2 side chains
18
Q

Describe the structure of an amino acid.

A

Amino acids are the basic monomer units which combine to make up a polymer called polypeptide.
Polypeptides can be combined to form proteins.

19
Q

What bonds are involved in the tertiary structure of proteins?

A
  • Disulfide bridges which are fairly strong
  • Ionic bonds which form between any carboxylate and amino group not involved in forming peptide bonds these are weaker than disulfide bridges.
  • Hydrogen bonds, lots but easily broken