The Raw Materials of Biotechnology

1
Chapter 2

• The Raw Materials of Biotechnology

2
Organisms and Their Components

• Organisms or their components
• Raw materials of biotechnology
• Maybe a molecule-HER2 antibody
• Maybe a cell- E. coli
• Maybe multice3llular
• Frost-resistant strawberry plants
• Receive resistance from insertion of gene from
  flounder which codes for a protein to help fish
  resist cold
• Must have thorough understanding of these
  organisms
• Normal development
• Interaction of chemical alterations with organism
  and environment
• . Biotechnicians need to be
• Cytologist (cell biologist)
• Anatomists (structure)
• Physiologists (function)

3
Organisms and Their Components

• The characteristics of Life
• Growth
• Reproduction
• Response to stimulus
• Metabolism
• Breakdown of food molecules for energy (cell
  respiration)
• Elimination of waste products
• Unicellular
• Only one cell
• Bacteria, protozoans, and algae
• Seen only with microscopes
• Critical for biotech applications

4
Organisms and Their Components

• Levels of Biological Organization
• Multicellular vs. unicellular
• Unicellular
• Bacteria, algae, protozoans
• Multicellular
• Plants, animals, fungi
• Multicellular grouped into functional levels

5
Organisms and Their Components

• Levels of Biological Organization
• Atoms
• Smallest units of matter
• Molecules
• Groups of atoms bonded together
• Organelles
• Structures in the cell that perform specialized
  functions
• Cells
• Basic unit of life
• The characteristics of a living organism

6
Organisms and Their Components

• Levels of Biological Organization
• Tissues
• Group of cells performing the same function
• Organs
• Different tissues that act together to perform a
  specific function
• Organ systems
• Organisms

7
Organisms and Their Components

• Levels of Biological Organization
• Why is this important to know?
• Necessary for the development/manufacture of a
  biotech product

8
Cellular Organization and Processes

• Cells
• Produce thousands of different molecules
• Exploited by biotech companies
• trick cells into producing target molecules in
  large amounts
• Then become products
• Insulin, hGH, etc
• From bacteria
• Plant cells
• No insulin
• Their own unique set of molecules are produced
• They are eukaryotic cells
• Same with animal cells
• Membrane bound organelles especially important
• Target of research and manufacturing

9
Cellular Organization and ProcessesPlant Cell
Structure
10
Cellular Organization and ProcessesPlant Cell
Structure

• Cell walls
• Provides main support
• Made of cellulose
• Paper
• Main part of dietary fiber
• Found in small quantities in bacteria
• None in animal cells

11
Cellular Organization and ProcessesAnimal Cell
Structure
12
Cellular Organization and Processes

• Types of Cells Used in Biotechnology
• CHO
• Vero cells
• African green monkey kidney epithelial cells
• HeLa cells
• Human epithelial cell
• Bacterial
• Prokaryotic
• No specialty organelles
• anaerobic
• E. coli
• Fungal or yeast
• Aspergillus
• No matter the type or source of cell
• Must know the cell to do proper culture techniques

13
Molecules of the Cell

• Four Classes of Organics
• Carbohydrates
• Monosaccharide
• Single sugar molecule
• Glucose, ribose, deoxyribose
• Disaccharides
• Contain two monosaccharides joined during
  dehydration reaction
• Sucrose
• Polysaccharides
• Polymers of monosaccharides
• Starch, cellulose, chitin

14
Synthesis and Degradationof Maltose, a
Disaccharide
15
StarchStructure and Function
16
GlycogenStructure and Function
17
CelluloseStructure and Function
18
Molecules of the Cell Lipids

• Lipids
• Insoluble in water
• Long chains of repeating CH2 units
• Renders molecule nonpolar
• Types of Lipids

19
Molecules of the Cell Lipids

• Triglycerides (Fats)
• Long-term energy storage
• Backbone of one glycerol molecule
• Three-carbon alcohol
• Each has an OH- group
• Three fatty acids attached to each glycerol
  molecule
• Long hydrocarbon chain
• Saturated - no double bonds between carbons
• Unsaturated - ?1 double bonds between carbons
• Carboxylic acid at one end
• Carboxylic acid connects to OH on glycerol in
  dehydration reaction

20
Dehydration Synthesis of Triglyceridefrom
Glycerol and Three Fatty Acids
21
Molecules of the Cell Lipids

• Phospholipids
• Derived from triglycerides
• Glycerol backbone
• Two fatty acids attached instead of three
• Third fatty acid replaced by phosphate group
• The fatty acids are nonpolar and hydrophobic
• The phosphate group is polar and hydrophilic
• Molecules self arrange when placed in water
• Polar phosphate heads next to water
• Nonpolar fatty acid tails overlap and exclude
  water
• Spontaneously form double layer a sphere

22
Phospholipids Form Membranes
23
Molecules of the Cell Lipids

• Steroids
• Cholesterol, testosterone, estrogen
• Skeletons of four fused carbon rings
• Waxes
• Long-chain fatty acid bonded to a long-chain
  alcohol
• High melting point
• Waterproof
• Resistant to degradation

24
Steroid Diversity
25
Waxes
26
Molecules of the CellProteins

• Functions
• Support Collagen
• Enzymes Almost all enzymes are proteins
• Transport Hemoglobin membrane proteins
• Defense Antibodies
• Hormones Many hormones insulin
• Motion Muscle proteins, microtubules

27
Molecules of the CellProteins

• Proteins are polymers of amino acids
• Each amino acid has a central carbon atom (the
  alpha carbon) to which are attached
• a hydrogen atom,
• an amino group NH2,
• A carboxylic acid group COOH,
• and one of 20 different types of R (remainder)
  groups
• There are 20 different amino acids that make up
  proteins
• All of them have basically the same structure
  except for what occurs at the placeholder R

28
Structural Formulas for the20 Amino Acids
29
ProteinsThe Polypeptide Backbone

• Amino acids joined together end-to-end
• COOH of one AA covalently bonds to the NH2 of the
  next AA
• Special name for this bond - Peptide Bond
• Two AAs bonded together Dipeptide
• Three AAs bonded together Tripeptide
• Many AAs bonded together Polypeptide
• Characteristics of a protein determined by
  composition and sequence of AAs
• Virtually unlimited number of proteins

30
Synthesis and Degradation of a Peptide
31
Protein MoleculesLevels of Structure

• Primary
• Literally, the sequence of amino acids
• A string of beads (up to 20 different colors)
• Secondary
• The way the amino acid chain coils or folds
• Describing the way a knot is tied
• Tertiary
• Overall three-dimensional shape of a polypeptide
• Describing what a knot looks like from the
  outside
• Quaternary
• Consists of more than one polypeptide
• Like several completed knots glued together

32
Levels of Protein Organization
33
Examples of Fibrous Proteins
34
Protein-folding Diseases

• Assembly of AAs into protein extremely complex
• Process overseen by chaperone molecules
• Inhibit incorrect interactions between R groups
  as polypeptide grows
• Defects in these chaperones can corrupt the
  tertiary structure of proteins
• Mad cow disease could be due to mis-folded
  proteins

35
Four Classes of Organics4 -Nucleic Acids

• Polymers of nucleotides
• Very specific cell functions
• DNA (deoxyribonucleic acid)
• Double-stranded helical spiral (twisted ladder)
• Serves as genetic information center
• In chromosomes
• RNA (ribonucleic acid)
• Part single-stranded, part double-stranded
• Serves primarily in assembly of proteins
• In nucleus and cytoplasm of cell

36
The Nucleotides ofNucleic Acids

• Three components
• A phosphate group,
• A pentose sugar (ribose or deoxyribose), and
• A nitrogenous base (4 kinds in DNA, 3 kinds in
  RNA, 3 common to both
• Nucleotide subunits connected end-to-end to make
  nucleic acid
• Sugar of one connected to the phosphate of the
  next
• Sugar-phosphate backbone

37
Nucleotides
38
DNA Structure
39
RNA Structure