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Functional Diversity of Proteins

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... Protein Structure Forces Involved in Protein Structure Primary Structure of Insulin Primary Structure of Lysozyme -Helix Secondary Structure -Structure ... – PowerPoint PPT presentation

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Title: Functional Diversity of Proteins


1
Functional Diversity of Proteins
  • Catalysis Enzymes amylase, pepsin, lipase
  • Transport hemoglobin, serum albumin
  • Structure keratin, collagen
  • Movement, Contraction myosin, actin
  • Defense antibodies, fibrinogen
  • Nutrient and Storage egg albumin, zein
  • Regulation hormones (insulin), repressors

2
Protein Classification by Function
Structure
Transport
Regulation
Motion
Catalysis
Regulation
Catalysis
Defense
Missing Function?
Storage
3
Classification of Proteins
By Shape
Fibrous -insoluble in water Functions
structure, motion High percentage of nonpolar
amino acids
Globular -usually soluble in water Functions
transport, catalysis, storage Higher percentage
of polar and charged amino acids
4
Classification of Proteins
By Composition
Simple contain only amino acids Examples
amylase, pepsin
Conjugated - contain something besides
amino acids Examples
Hemoglobin - contains iron Immunoglobin -
contains carbohydrate Lactate
dehydrogenase - contains niacin
5
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6
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7
Nonpolar Amino Acids
8
Polar, Uncharged Amino Acids
9
Polar, Charged Amino Acids
Negatively-charged
Positively-charged
10
Amino Acid Classification Functional Group
Sulfhydryl
Alcohol
Carboxylic Acid
Amide
11
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12
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13
?-carboxyl group
?-carbon
side chain
?-amino group
14
Amino Acid Titration
Below Isoelectric pH Net Charge
Above Isoelectric pH Net Charge
Isoelectric pH Net Charge 0
15
Titration of Glycine
16
Titration of Glutamic Acid
17
Titration of Histidine
18
Electrophoresis of Amino Acid Mixture at pH
6 Alanine, Arginine, Aspartic Acid
At pH 6
Alanine (pI 6)
Net charge 0
Arginine (pI 10.8)
Net charge is
Net charge is
Aspartic Acid (pI 2.8)
19
Paper Chromatography of Amino Acids
Tyr
Phe
Leu
Gly
Asp
Lys
polar amino acids
nonpolar amino acids
20
Biologically Active Peptides
Impact of changes in amino acids
Vasopressin - Stimulates water reabsorption in
the kidney
Oxytocin - Stimulates lactation and uterine
contraction
21
Levels of Protein Structure
22
Forces Involved in Protein Structure
23
Primary Structure of Insulin
24
Primary Structure of Lysozyme
25
Secondary Structure
?-Helix
26
Secondary Structure
?-Structure
27
Collagen (triple helix)
28
Elastin Structure
29
Myoglobin Secondary and Tertiary Structure
??- helix
??- helix
30
Myoglobin
31
Lysozyme Secondary and Tertiary Structure
??- helix
??- structure
32
Lysozyme Tertiary Structure
33
Hemoglobin Quaternary Structure
Heme Group
34
Sickle-cell Hemoglobin
valine-valine interaction
35
Electrophoresis of Hemoglobin A, Sickle-Cell
Hemoglobin, and Hemoglobin C
Hemoglobin S Glu to Val at Position 6 on the
Beta Chain
Hemoglobin C Glu to Lys at Position 6 on the
Beta Chain
36
Protein Denaturation
  • Denaturation involves
  • The disruption of bonds in the secondary,
    tertiary and quaternary protein structures.
  • Heat and organic compounds that break apart H
    bonds and disrupt hydrophobic interactions.
  • Acids and bases that break H bonds between polar
    R groups and disrupt ionic bonds.
  • Heavy metal ions that react with S-S bonds to
    form solids.
  • Agitation such as whipping that stretches peptide
    chains until bonds break.

37
Applications of Denaturation
  • Use of 70 ethanol or isopropyl alcohol as a
    disinfectant
  • Use of silver nitrate solution in eyes of
    newborns to
  • prevent gonorrhea infection
  • Use of eggs or milk as antidote for heavy metal
    poisoning
  • Use of tannic acid in burn ointment to coagulate
    proteins
  • at burn site
  • Use of high temperature to sterilize items

38
Denaturation and Renaturation of Ribonuclease
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