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Proteins

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Proteins * It s a helix or B sheet within a single region. Can have both in one protein but a specific region is one or another * How the whole thing holds together ... – PowerPoint PPT presentation

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Title: Proteins


1
Proteins
2
  • Proteins

Multipurposemolecules
3
Proteins
  • Most structurally functionally diverse group of
    biomolecules
  • Function
  • involved in almost everything
  • enzymes (pepsin, polymerase, etc.)
  • structure (keratin, collagen)
  • carriers transport (membrane channels)
  • receptors binding (defense antibodies)
  • contraction (actin myosin)
  • signaling (hormones insulin)
  • storage (bean seed proteins)

4
Proteins
  • Structure
  • monomer amino acids
  • 20 different amino acids
  • polymer polypeptide
  • protein can be one or more polypeptide chains
    folded bonded together
  • large complex molecules
  • complex 3-D shape

hemoglobin
growthhormones
5
Amino acids
  • Structure
  • central carbon
  • amino group
  • carboxyl group (acid)
  • R group (side chain)
  • variable group
  • confers unique chemical properties of the amino
    acid

R
6
Nonpolar amino acids
7
Polar amino acids
8
Sulfur containing amino acids
  • Form disulfide bridges
  • cross links betweens sulfurs in amino acids

H-S S-H
You wonderedwhy permssmelled like rotten eggs?
9
Building proteins
  • Peptide bonds
  • linking NH2 of one amino acid to COOH of another
  • CN bond

dehydration synthesis
10
Protein structure function
  • Function depends on structure
  • 3-D structure
  • twisted, folded, coiled into unique shape

pepsin
11
Primary (1) structure
  • Order of amino acids in chain
  • amino acid sequence determined by gene (DNA)
  • slight change in amino acid sequence can affect
    proteins structure its function
  • even just one amino acid change can make all the
    difference!

lysozyme enzyme in tears mucus that kills
bacteria
12
Sickle cell anemia
13
Secondary (2) structure
  • Local folding
  • folding along short sections of polypeptide
  • interaction between adjacent amino acids
  • H bonds between R groups
  • ?-helix
  • ?-pleated sheet

14
Tertiary (3) structure
  • Whole molecule folding
  • determined by interactions between R groups
  • hydrophobic interactions
  • effect of water in cell
  • anchored by disulfide bridges(H ionic bonds)

15
Quaternary (4) structure
  • More than one polypeptide chain joined together
  • only then is it a functional protein
  • hydrophobic interactions

collagen skin tendons
hemoglobin
16
Protein structure (review)
R groups hydrophobic interactions, disulfide
bridges
3
1
2
4
17
  • Lets build some
  • Proteins!

18
Protein models
  • Protein structure visualized by
  • X-ray crystallography
  • extrapolating from amino acid sequence
  • computer modelling

lysozyme
19
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