Functional Diversity of Proteins u Catalysis: Enzymes: amylase, pepsin, lipase u Transport: hemoglobin, serum albumin u Nutrient and Storage: egg albumin,

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Presentation transcript:

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

Protein Classification by Function Structure Regulation Motion Regulation Transport Defense Catalysis Missing Function?Storage

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

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

 -carbon  -amino group  -carboxyl group side chain

Nonpolar Amino Acids

Polar, Uncharged Amino Acids

Polar, Charged Amino Acids Negatively-charged Positively-charged

Amino Acid Classification: Functional Group Alcohol Amide Carboxylic Acid Sulfhydryl Threonine (Thr)Serine (Ser) Cysteine (Cys) Aspartic Acid (Asp) Glutamic Acid (Glu) Asparagine (Asn) Glutamine (Gln)

 -carbon  -amino group  -carboxyl group side chain

Amino Acid Titration Isoelectric pH Net Charge 0 Below Isoelectric pH Net Charge + Above Isoelectric pH Net Charge –

Titration of Glycine Isoelectric pH = 6.0

Titration of Glutamic Acid Isoelectric pH = 3.2

Titration of Histidine Isoelectric pH = 7.6

Electrophoresis of Amino Acid Mixture at pH 6 Alanine, Arginine, Aspartic Acid At pH 6 Alanine (pI = 6)Net charge = 0 Aspartic Acid (pI = 2.8) Net charge is – Arginine (pI = 10.8)Net charge is +

Paper Chromatography of Amino Acids polar amino acidsnonpolar amino acids TyrPheLeuGlyAspLys

Biologically Active Peptides Vasopressin - Stimulates water reabsorption in the kidney Oxytocin - Stimulates lactation and uterine contraction Impact of changes in amino acids

Levels of Protein Structure

Forces Involved in Protein Structure

Primary Structure of Insulin

Primary Structure of Lysozyme

 -Helix Secondary Structure

 -Structure Secondary Structure

Collagen (triple helix)

Elastin Structure

Myoglobin: Secondary and Tertiary Structure  - helix

Myoglobin Surface View Cross-Section Heme Group

Lysozyme: Secondary and Tertiary Structure  - helix  - structure

Lysozyme: Tertiary Structure Active Site

Hemoglobin: Quaternary Structure Heme Group

Sickle-cell Hemoglobin valine-valine interaction

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

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.

Applications of Denaturation  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  Use of 70% ethanol or isopropyl alcohol as a disinfectant

Denaturation and Renaturation of Ribonuclease