Proteins Flashcards

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1
Q

What are amino acids?

A

The monomers from which proteins are made.

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2
Q

What are proteins?

A

Polymers

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3
Q

What is the general structure of an amino acid?

A

Where NH2 represents an amine group, COOH represents a carboxyl group and R represents a side chain. The twenty amino acids that are common in all organisms differ only in their side group.

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4
Q

How is a peptide bond formed?

A

A condensation reaction between two amino acids.

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5
Q

How are dipeptides formed?

A

Formed by the condensation of two amino acids.

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6
Q

How are polypeptides formed?

A

Formed by the condensation of many amino acids.

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7
Q

How are amino acids joined together to form a dipeptide?

A
  • condensation reaction
  • water is removed
  • peptide bond forms between OH of carboxyl and H of amine group.
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8
Q

Does a functional group only contain one polypeptide?

A

They may contain one or more polypeptides.

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9
Q

What are the 4 levels in a protein?

A

Primary, Secondary, Tertiary, Quaternary

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10
Q

What is a primary structure?

A

The order of the amino acids in a polypeptide chain - this is a polymer
TIP = THE SEQUENCE IS VITAL-YOU CANNOT JUST SAY A CHAIN OF AMINO ACIDS.

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11
Q

What is a secondary structure?

A
  1. The structure of amino acids causes parts of a protein molecule to bend into α shape or fold into β pleated sheets.
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12
Q

How do hydrogen bonds relate to the secondary structure?

A
  • Hydrogen bonds hold the secondary structure.
  • Hydrogen bonds form between the C=O groups of the carboxyl groups of one amino acids and the H in the amine group of another amino acid.
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13
Q

What is the tertiary structure?

A
  1. The further folding of the secondary structure.
  2. To form a unique 3D shape.
  3. Held in place by ionic, disulfide, and hydrogen bonds.
    - The ionic and disulfide bonds form between the R groups of the different amino acids.
    - The disulfide bonds only sometimes occur, as there must be a sulfur in the R groups for this bond to occur.
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14
Q

What is the quaternary structure?

A
  • A protein made up of one or more polypeptide chains. e.g. haemoglobin is made up of 4 polypeptide chains.
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15
Q

Conditions that denature a protein?

A
  • too high temperature ( too much kinetic energy)
  • too high/low a pH.
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16
Q

What happens when a protein is denatured?

A

When a protein is denatured, this means that bonds that hold the tertiary and secondary structure in shape break, and therefore the unique 3D shape is lost ( e.g. enzymes lose their unique active site shape ).

17
Q

What is the importance of the primary structure?

A
  • If even one amino acid in the sequence is different then it will cause the ionic, disulfide, and hydrogen bonds to form in different locations. This results in different 3D shapes.
18
Q

What is the impact of a primary structure?

A

Enzymes will have a differently shaped active site ( will be non - functioning ).
Carrier proteins will have a different shape binding site (molecules are complementary and cannot be transported across membranes ).