Protein Folding Protein Folding Proteins have unique 3-dimensional - - PowerPoint PPT Presentation

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Protein Folding Protein Folding Proteins have unique 3-dimensional - - PowerPoint PPT Presentation

Protein Folding Protein Folding Proteins have unique 3-dimensional shapes created by the twisting or folding of one or more polypeptide chains The structure of a protein enables it to recognize and bind to other molecules Protein


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SLIDE 1

Protein Folding

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SLIDE 2

Protein Folding

  • Proteins have unique 3-dimensional shapes

created by the twisting or folding of one or more polypeptide chains

  • The structure of a protein enables it to

recognize and bind to other molecules

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SLIDE 3

Protein Folding

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SLIDE 4

Shape Determines Function

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SLIDE 5

Shape Determines Function

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SLIDE 6

Shape Determines Function

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SLIDE 7

Protein Structure

  • Primary Structure
  • Secondary Structure
  • Tertiary Structure
  • Quaternary Structure
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SLIDE 8

Primary Structure

  • Determined by the sequence of a chain of

amino acids held together by peptide bonds

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SLIDE 9

Secondary Structure

  • Involves regions of coiling (α-helices) or

folding (β-pleated sheets) of the polypeptide

  • Stabilized by hydrogen bonds between the

carboxyl and amino groups of amino acids

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SLIDE 10

Tertiary Structure

  • Results from interactions between the various

side chains (R groups)

  • Ionic bonds between positive (+) and negative

(-) side chains

  • Hydrophobic interactions between nonpolar

side chains (repelled by water), clump together

  • Hydrogen bonds between polar side chains
  • Disulfide bridges between the sulfhydryl groups
  • f cysteine amino acids
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SLIDE 11
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SLIDE 12

Tertiary Structure

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SLIDE 13

Quaternary Structure

  • Occurs in proteins that are composed of more

than one polypeptide

  • Results from the combination of hydrogen

bonding, ionic bonding, and hydrophobic interactions between polypeptide chains

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SLIDE 14

Protein Folding Control

  • Chaperones and proteasomes are molecules

that act jointly to regulate protein folding and control the selective removal of misfolded proteins from the cell

  • Chaperones control the conformational

folding and unfolding of proteins released from ribosomes

  • Proteasomes degrade unneeded or damaged

proteins

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SLIDE 15
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SLIDE 16

Diseases Caused by Misfolded Proteins

  • Alzheimer’s Disease
  • Parkinson’s
  • Amyotrophic lateral sclerosis (ALS)
  • Huntington’s Disease
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SLIDE 17

Sickle-Cell Anemia Mutation

  • Causes hemoglobin molecules to crystallize

when oxygen levels are low

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SLIDE 18

Insulin Receptor – Type 2 Diabetes