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Protein Folding Notes.

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Presentation on theme: "Protein Folding Notes."— Presentation transcript:

1 Protein Folding Notes

2 Protein Structure = Protein Function
In order to perform its specific job in the cell, a protein must fold into its proper shape

3 Levels of Protein Folding
Primary The order of amino acids in a polypeptide chain

4 Levels of Protein Folding
Secondary Folding caused by interactions within the protein’s backbone β pleated sheet α helix

5 Levels of Protein Folding
Tertiary Folding caused by bonding between amino acid R groups Opposites (positive and negative) attract Cysteine covalently bonds with other cysteines Hydrophobic amino acids move to the middle Hydrophilic amino acids move to the outside

6 Tertiary Structure

7 Levels of Protein Folding
Quaternary Individual polypeptide chains come together to form a multi-subunit protein

8 Watch Proteins Fold! amino-acids.json

9 To Sum Up

10 Make a Protein! Positively Charged Negatively Charged Hydrophilic
Hydrophobic Histidine Aspartic Acid Serine Methionine Arginine Glutamic Acid Threonine Glycine Lysine Glutamine Tyrosine Proline Isoleucine Asparagine Leucine Cysteine  Alanine Valine Phenylalanine Tryptophan


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