5.2.1

Structure & Functions of Proteins

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Polypeptides

Amino acids are the monomers that join together to form polymers called polypeptides (proteins).

Structure of proteins

Structure of proteins

  • Proteins are made up of amino acids.
  • Dipeptides are formed from the condensation of two amino acids.
  • Polypeptides are formed by the condensation of many amino acids.
Structure of amino acids

Structure of amino acids

  • Each amino acid has a central carbon atom (alpha carbon).
  • There are four atoms or groups of atoms bonded to the central carbon atom:
    • NH2 (an amine group).
    • COOH (a carboxyl group).
    • H (a hydrogen atom).
    • R (a side group).
R groups

R groups

  • The R group is different in each amino acid.
  • The R group determines how the amino acid interacts and bonds with other amino acids in the polypeptide.
Essential amino acids

Essential amino acids

  • There are 20 different types of amino acids that are common in all organisms.
    • 10 of these are essential amino acids in humans because the human body cannot produce them and they are obtained from the diet.
Glycine

Glycine

  • Glycine is an example of an amino acid.
  • Glycine has a hydrogen atom in its R group.
  • Glycine is the only amino acid that does NOT have a carbon atom in its R group.

Peptide Bond

Each amino acid is attached to another amino acid as a result of a condensation reaction. These reactions cause peptide bonds to form.

Polypeptides

Polypeptides

  • Polypeptides are made from chains of amino acids.
  • There are amino acids at each end of the polypeptide chain.
  • These amino acids form the two end terminals:
    • The N-terminal (amine terminal).
    • The C-terminal (carboxyl terminal).
The peptide bond

The peptide bond

  • When two amino acids react together, a bond forms between the carboxyl group of one amino acid and the amine group of a second amino acid.
  • One water molecule is released as a by-product.
  • The bond formed between two amino acids is a covalent bond called a peptide bond.

Function of Proteins

Proteins have a diverse range of functions. Each cell in a living system may contain thousands of proteins, each with a unique structure and function. Functions of proteins include:

Enzymes

Enzymes

  • Enzymes are biological catalysts.
  • Enzymes increase the rate of a reaction without being used up in the reaction.
  • The enzymes are usually tightly folded, complex proteins that are soluble.
Antibodies

Antibodies

  • Antibodies are made up of polypeptide chains.
  • Antibodies are used in the immune response.
  • Antibodies are diverse proteins.
    • Each antibody has a different sequence of amino acids.
Transport proteins

Transport proteins

  • Transport proteins include channel proteins.
  • Channel proteins transport molecules across the cell membrane.
  • Channel proteins transport molecules that are too large to diffuse freely or molecules that carry a charge.
Structural proteins

Structural proteins

  • Structural proteins are long, strong polypeptide chains.
  • Structural proteins are connected by cross-links that hold the chains parallel to each other.
    • E.g. Collagen and keratin.
Jump to other topics
1

Unity & Diversity - Molecules

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Unity & Diversity - Cells

3

Unity & Diversity - Organisms

4

Unity & Diversity - Ecosystems

5

Form & Function - Molecules

6

Form & Function - Cells

7

Form & Function - Organisms

8

Form & Function - Ecosystems

9

Interaction & Interdependence - Molecules

10

Interaction & Interdependence - Cells

11

Interaction & Interdependence - Organisms

12

Interaction & Interdependence - Ecosystems

12.1

Populations & Communities

12.2

Transfers of Energy & Matter

13

Continuity & Change - Molecules

14

Continuity & Change - Cells

15

Continuity & Change - Organisms

16

Continuity & Change - Ecosystems

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