3.6 Structure of Proteins Flashcards

1
Q

What is the monomer of proteins?

A

Amino acids

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2
Q

What bonds form when amino acids join?

A

Peptide bond

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3
Q

What elements are in proteins?

A

Carbon, hydrogen, oxygen, nitrogen

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4
Q

What is the role of proteins?

A

-Enzymes = used to break down and synthesise molecules
-Antibodies = immune response
-Transport = move molecules or ions across membranes
-Structural components = keratin, collagen used to create strong fibres
-Muscle contraction = muscles are made up of proteins
-Hormones = act as chemical messengers

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5
Q

What is the general structure of an amino acid?

A

-Central carbon atoms
-A amino group (NH2)
-A carboxyl group (COOH)
-A hydrogen atom
-An R group or a variable side group

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6
Q

What does the R group determine?

A

-Which amino acid it is, and its properties
-R groups are able to interact with each other forming different types of bond, leading to long chains of amino acids

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7
Q

How is a dipeptide formed?

A

-Condensation reaction of two amino acids
-The hydroxyl group (OH) of one amino acid reacts with the hydrogen (H) in the amino group of another amino acid
-Releases a water molecules
-Forms a peptide bond between the carbon of one amino acid and the nitrogen of another

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8
Q

How is a dipeptide broken down?

A

-Hydrolysis reaction
-Water molecule is added to dipeptide
-Peptide bond is broken
-Release two amine acids

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9
Q

What is the name of the molecules formed when more than two amino acids join?

A

Polypeptide

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10
Q

How are dipeptide and polypeptides broken down?

A

Hydrolysis

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11
Q

What are the 4 levels of protein structure?

A

Primary, Secondary, Tertiary, Quaternary

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12
Q

What is the name of test for proteins?

A

Biuret test

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13
Q

What does the Biuret test test for?

A

Presence of amino acids

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14
Q

What are the steps for the Biuret test?

A
  1. Place 4cm3 of food sample in a test tube
  2. Add an equal volume of Biuret solution (sodium hydroxide and copper sulfate)
  3. Shake and leave at room temperature
  4. If proteins are present, solution will turn from a blue solution to a purple precipitate
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15
Q

What is Biuret solution made from?

A

Sodium hydroxide and copper sulfate

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16
Q

What is the primary structure of a protein?

A

-The unique sequence in which amino acids are jointed
-Structure held together by peptide bonds
-Determines the 3D shape
-A change in just one of the amino acids can result in a change to the proteins structure and function

17
Q

What bonds are in the primary structure of a protein?

18
Q

What is the secondary structure of a protein?

A

-Hydrogen bonds forming between amino acids in the chain
-Polypeptide chain coils/fold into either an α-helix or β-pleated sheet structure
-Many hydrogen bonds make the structure stable
-α-helix formed due to hydrogen bonds within the amino acids chain, pulling it into a coil shape
- β-pleated sheet structure formed by hydrogen bonds between parallel amino acids

19
Q

What bonds are in the secondary structure of a protein?

A

Hydrogen bonds

20
Q

What is the tertiary structure of a protein?

A

-3D shape of a polypeptide chain, caused by the folding and twisting of a protein
-Coiling and folding causes R-groups of different amino acids to become closer together, so they can interact
-Hydrophobic and hydrophilic interactions, weak interaction between polar and non-polar R groups
-Hydrogen bonds, weak individually but provide strength in large numbers
-Ionic bonds, form between oppositely charged R groups, stronger than hydrogen bonds
-Disulfide bridges, form between R groups that contain sulfur, covalent and the strongest of bonds

21
Q

Where do ionic bonds form in the tertiary structure of a protein?

A

Between oppositely charged R-groups

22
Q

Where do disulfide bridges form in the tertiary structure of a protein?

A

Between R groups that contain sulfur

23
Q

Where do hydrophobic and hydrophilic interactions take place in the tertiary structure of a protein?

A

Between polar and non-polar R groups

24
Q

What bonds are present in the tertiary structure of a protein?

A

Hydrophobic and hydrophilic interactions, Hydrogen bonds, Ionic bonds, Disulfide bridges

25
What proteins are tertiary in structure?
Enzymes, antibodies, some hormones
26
What is the Quaternary structure of a protein?
-Two or more polypeptide chains held together (association of two or more individual proteins called subunits) -Interactions between polypeptide chains (subunits) are same as in the tertiary structure -Can also involve the addition of non-protein groups known as are prosthetic groups
27
What bonds occur in the tertiary structure of a protein?
Hydrophobic and hydrophilic interactions, Hydrogen bonds, Ionic bonds, Disulfide bridges
28
Examples of quaternary proteins?
Haemoglobin, antibodies
29
Where are hydrophobic and hydrophilic interactions in proteins?
Hydrophilic grows are on the outside of the protein, hydrophobic groups are on the inside of the molecule shielded from the water in the cytoplasm
30