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Comparison of Abilities
Human eye
Light microscope
Transmission Electron Microscope
Levels of OrganisationLiving Organisms
systems
organs
tissues
cells
Biomolecules
Organic
carbohydrates proteins lipids nucleic acids
Inorganic IonsWater
(inorganic)
Levels of OrganisationBiomolecules
Organic
carbohydrates proteins lipids nucleic acids
Inorganic IonsWater
(inorganic)
simple sugars amino acids fatty acids nucleotides
glycerol
The nature of the cell
Intracellular aqueous environment
Extracellular aqueous environment
Cell boundary or plasma membrane
• Insoluble• Semi-permeable
What all cells need to do
Make specific Biomacromolecules
Control and regulate chemicalReactions
Produce energy to drive Chemical reactions
Take in small moleculesProduce useful products for export from the cell
Receive and respond to
chemical signalsRemove waste
products
Grow, reproduce and pass on genetic information to the next generation of cells
Cell structure needs to meet the needs of molecules
• The processes within a cell are due to molecules interacting with each other
• Molecules need to move into and around the cell at a certain rate to reach sites of specific activity
• Molecules need to be in adequate concentrations if chemical reactions are going to occur at the right rate
• Cell structure needs to facillitate the movement of molecules and maintain them in adequate concentrations so reactions can occur to maintain cell functioning
Why size and shape matters• Cells need to maximise their surface area to ensure the rapid
movement of of molecules. This becomes a problem as the volume of the cell increases. Size does matter!
Shape A B C
L x W x H 1x1x1 10x10x
10
10x100x1
Surface Area (6a2)
6 600 2200
Volume (a3)
1 1000 1000
SA:V
(SA/V)
6 0.6 2.2
A
B
C
So how do organisms deal with having cells with an insufficient
SA:V to facilitate the transport of molecules?
• ORGANELLES!• Each of the intracellular organelles will be
studied this semester, but the emphasis will be on their various functions, and how they compensate for the relatively large volumes of eukaryotic cells
• Prokaryotic cells being smaller, do not have this necessity
Animal Cells
Plant Cells
The functions of organelles:
• Movement of substances across the plasma membrane
• The protein secretory pathway
• Photosynthesis
• Cellular respiration
• The signal transduction pathway
• Aspects of the immune response
• Packaging and export of cellular products
A little chemistry …
Covalent bonding
involves atoms joining to form
molecules
In order to form a stable molecule, each atom must share sufficient
electrons in order to result in a full outer
shell
If an atom only has one shell of electrons, 2 is sufficient to fill it
The second shell and onwards all require a minimum of 8
electrons in order to achieve stability
Oxygen has an atomic
number of 8
Hydrogen has an atomic
number of 1
A little chemistry …… and a hydrogen
atom contains 1 proton and 1 electron
So an oxygen atom contains 8 protons
and 8 electrons
A little chemistry …
When oxygen and hydrogen bond, the
hydrogen is stable, it has a full outer shell
… but the oxygen is still left short one
electron
A little chemistry …
This allows an additional hydrogen
atom to bond with the oxygen
… thus creating a stable molecule
A little chemistry …
Thus we achieve the structure of a water
molecule: One oxygen atom bonded
to two hydrogen atoms
How water interacts with other substances
• If a substance is composed of charged atoms, these will be attracted to the negatively charged oxygen atom or the positively charged hydrogen atoms. These are known as polar or hydrophyllic.
• If a substance has no charge, then it will not be able to interact with the water molecules. These are known as non-polar or hydrophobic.
pH
• pH is simply a measure of the number of hydrogen ions vs the number of hydrogen ions in a solution.
• More H+ = lower pH (0-6) = acidic• More OH- = higher pH (8-14) = basic• Equal H+ and OH- = pH 7 = neutral
Water molecules are cohesive -> they form hydrogen bonds
Substances that dissolve in water are called hydrophilic or polar
Substances that are insoluble in water are called hydrophobic or non-polar
Monomers: Polymers:
Sugars Carbohydrates (Polysaccharides)
Amino Acids Proteins
Fatty acids & glycerol Lipids
Nucleotides Nucleic Acids
From molecules to biomacromolecules• Biomacromolecules are giant molecules.
They play essential roles in both the structure and function of cells
• Cells import water, mineral ions and a host of small organic molecules like simple sugars, fatty acids and amino acids.
• In contrast, cells can only acquire biomacromolecules by making them. They are made in a condensation reaction.
Glucose, Fructose Sucrose, LactoseStarch, Glycogen & Cellulose
hexose shape pentose shape
Mostly ends in –ose
C, H, O => organic
Condensation reaction
• Monomers are flanked by a hydroxide and a hydroxyl group• When the reaction is facilitated by an enzyme, they will
come together in the correct alignment
The Condensation Reaction
MonomerH - O O - H MonomerH - O O - H
• The correctly aligned interaction of the hydroxide group of one monomer with the hydroxyl group of another will cause the molecules to join, with water as a by-product
The Condensation Reaction
MonomerH - O O - H MonomerH - O O - HH2O
• The end result is a larger molecule, with its two monomers joined by an oxygen bridge
The Condensation Reaction
MonomerH - O MonomerO O - H
• This is simply the opposite to a condensation reaction• When an enzyme exerts pressure on the large molecule, the oxygen
bridge is put under stress• This allows water to enter the bond
Hydrolysis
MonomerH - O MonomerO O - HH2O
• One of the hydrogen atoms attaches to the oxygen, whilst the other oxygen and hydrogen attach to the other monomer in the form of a hydroxyl group.
• The larger molecule has been divided in to two smaller subunits
Hydrolysis
MonomerH - O O - H MonomerH - O O - HH2O
Energy storage• In Animals
• Food broken down to glucose• Excess glucose stored as glycogen• Excess glycogen stored as fat
• In Plants• Glucose produced via photosynthesis• Glucose combined with fructose to form sucrose• Sucrose transported to other parts of plant• Excess sucrose stored as starch
Lipids• Comprised of two types of subunits:
• Fatty acids• Glycerol
• Molecules contain less water than carbohydrates, so can contain more energy
• Thus lipids are a very important energy store for animals
Triglycerides
Phospholipids
How the monomers interact• The reason that lipids are not polymers is that
there is only one gycerol subunit with three carbon atoms on to which the fatty acid chains can attach.
• In triglycerides, one chain attaches to each of the three carbon atoms
• In phospholipids, one of the carbons is taken up by a phosphate group, therefore there is only space for two fatty acid chains
Other than phospholipids, which contain P, most others will only contain C, H & O
DNA: deoxyribonucleic acidRNA: ribonucleic acid
SUGAR
PHOSPHATE
Nucleic acids contain C, H & O in addition to N & P
DNA:Adenine (A)Thymine (T)Cytosine (C)Guanine (G)
RNA:Adenine (A)Uracil (U)Cytosine (C)Guanine (G)
Differences between DNA & RNA
DNA RNA
A, C, G, T A, C, G, U
Paired strands Single strand
H+ at 2’ OH- at 2’
Summary of animation• mRNA copy of gene on DNA made in nucleus
• mRNA swims out to ribosome (made from rRNA) in cytoplasm
• Ribosome reads code, for every 3 base pairs, 1 amino acid is added to the chain
• Amino acids are brought to the ribosome by tRNA transfer molecules
• Once process is complete, protein is released from the ribosome.
3 groups: Amino group, Carboxyl group & R-group
When joined together they form peptide bonds
Aside from the C, H, O & N in the base molecule, the R group may also contain S & P
Protein structure• Primary structure
• The linear sequence of amino acids
• Secondary structure• The type of peptide bond determines how sections of the
protein fold – spiral helix / pleated sheet / random coils• Shape reinforced by additional H bonds
• Tertiary structure• Eventual 3D shape formed by folding• Shape reinforced by additional H bonds
• Quanternary structure• When a protein is formed by the interaction of 2 or more
polypeptide chains
Primary structure: Secondary structure:
Tertiary structure:
Quaternary structure:
Active vs inactive proteins• Not all proteins are produced in an active form• Often they will need to be activated by a specific
enzyme (also a protein)• In the case of the hormone insulin, it will only be
activated when a disulphide bond is broken in the active site of the activating enzyme, thereby releasing one of its 3 polypeptide chains
• So in our study of proteins, knowing the action of one is often not helpful, we need to know the make-up of the organism’s entire proteome.
Biomacromolecule
Type of bonding
Carbohydrates Glycosidic bond
Lipids Ester bond
Nucleic acids Phosphodiester bond
Proteins Peptide bond