1. Intro
1.1. Catabolic Reactions
1.1.1. Larger molecules into smaller molecules
1.2. Anabolic Reactions
1.2.1. Joining smaller molecules into larger ones
1.3. Monomers
1.3.1. Single small molecules
1.4. Polymers
1.4.1. A larger molecule made up of more than two or more similar monomers
1.5. Condensation reaction
1.5.1. The chemical reaction that contains biological monomers
1.5.1.1. Covalent bond formed
1.5.1.2. Water molecule released
1.5.1.3. A larger molecule is formed by joining smaller ones
1.6. Hydrolysis reaction
1.6.1. Splitting larger molecules into smaller ones
1.6.1.1. Covalent bond broken
1.6.1.2. Molecule of water used
1.6.1.3. Smaller molecules are formed
2. Carbohydrates
2.1. Consists of carbon, hydrogen and oxygen
2.2. Monosaccharides
2.2.1. Simple sugars like glucose, fructose and ribose
2.2.2. General formula
2.2.2.1. (CH2O)n
2.2.3. Soluble in water
2.2.4. Sweet tasting
2.2.5. Forms crystals
2.2.6. Alpha glucose
2.2.7. Beta Glucose
2.3. Disaccharides
2.3.1. Two monosaccharide sugars join together to form a disaccharide
2.3.2. Water molecule is removed and a covalent bond called a Glycosidic bond is formed
2.3.3. Maltose
2.3.3.1. Glucose + Glucose
2.3.4. Sucrose
2.3.4.1. Glucose + Fructose
2.3.5. Lactose
2.3.5.1. Glucose + Galactose
2.4. Polysaccharides
2.4.1. Polymers formed by combining many monosaccharide molecule by glycosidic bonds
2.4.2. Insoluble
2.4.3. Compact
2.4.4. Can be hydrolysed to form alpha glucose monomers which can be easily transported and used in respiration
2.4.5. Starch
2.4.5.1. Amylose
2.4.5.1.1. Alpha Glucose monomers
2.4.5.1.2. 1,4 glycosidic bonds
2.4.5.1.3. Coiled chains
2.4.5.2. Amylopectin
2.4.5.2.1. Alpha Glucose monomers
2.4.5.2.2. 1,4 Glycosidic bonds
2.4.5.2.3. 1,6 Glycosidic bonds
2.4.5.2.4. Branched
2.4.5.3. Found in plants
2.4.6. Glycogen
2.4.6.1. Found in animals and bacteria
2.4.6.2. Highly branched
2.4.6.3. 1,4 glycosidic bonds
2.4.6.4. 1,6 glycosidic bonds
2.4.6.5. Alpha glucose monomers
2.4.7. Cellulose
2.4.7.1. Beta glucose monomers
2.4.7.2. Found in plants
2.4.7.3. 1,4 glycosidic bonds
2.4.7.4. Each monomer rotated 180 degrees
2.4.7.5. Linear chains
2.4.7.6. Hydrogen bonds between the OH- groups to form bundles called microfibrils
3. Properties of Water
3.1. Small dipolar molecule
3.2. Hydrogen bond formed and broken continuously
3.3. Metabolic role
3.3.1. Condensations and hydrolysis reaction
3.3.2. Joining amino acids together by peptide bonds by condensation reactions forming polypeptides
3.3.3. Splitting disaccharides to monosaccharides by hydrolysis reactions
3.4. High Latent Heat of Vapourisation
3.4.1. Requires huge amounts of energy to break the hydrogen bonds
3.4.2. "Cooling effect"
3.5. Liquid with Relatively High Boiling Point
3.5.1. Continuous making and breaking of bonds
3.5.2. Water molecule is not a gas but a liquid
3.6. Low Density of Ice
3.6.1. The bonds allow the molecules to spread out more
3.7. High Specific Heat Capacity- Thermostability
3.7.1. Relatively large amounts of energy is required to increase the temp. of water
3.7.2. Large bodies of water are thermostable when there are large fluctuations of temps.
3.7.2.1. Doesn't change temp.
3.8. Cohesion
3.8.1. Hydrogen bonds cause water molecules to stick together
3.8.2. Surface tension
3.8.3. Adhesion
3.8.3.1. When water molecules stick to other surfaces
3.8.3.1.1. E.g.
3.9. Solvent
3.9.1. Polarity of water allows other polar molecules to dissolve in water
3.10. Transport medium
3.10.1. Stays a liquid and allows other molecules to be carrie in it
3.11. Transparent
3.11.1. Photosynthesis for water plants
4. Lipids
4.1. Triglycerides and phospholipids are two groups of lipids
4.2. Contains carbon hydrogen and oxygen
4.3. NOT polymers
4.4. Triglycerides
4.4.1. One molecule of glycerol joined by covalent ester bonds formed in condensation reactions to three fatty acids
4.4.1.1. 3 molecules of water realeased
4.4.2. Source of energy
4.4.3. Act as insulators
4.4.4. Insoluble in water
4.4.5. Protection fat
4.4.5.1. Shock absorbers for organs
4.4.6. Saturated fatty acids
4.4.6.1. NO double bonds
4.4.6.2. Linear chains
4.4.7. Unsaturated fatty acids
4.4.7.1. Double bonds
4.5. Phospholipids
4.5.1. Found in cell membranes
4.5.2. Contains a glycerol molecule and two fatty acids with the third fatty acid replaced by a phosphate group
4.5.3. Electrically charged/ Polar
4.5.4. Hydrophilic
5. Inorganic Ions
5.1. The more H+ ions the more acidic the solution
5.2. Haemoglobin
5.2.1. Four subunits found in erythrocytes
5.2.2. Each subunit has polypeptide chain and a non-protein haem group
5.2.2.1. Contains a single iron atom in the form Fe+
5.2.3. The harm group has a high affinity for oxygen
5.3. Co-transporters
5.3.1. specialised inartistic proteins span the phospholipid bilayer
5.4. Phosphate ion
5.4.1. DNA, RNA, ATP
5.4.2. Allow phosphodiester bonds to form between nucleotides forming polynucleotides
6. Enzymes
6.1. Tertiary proteins with a globular shape
6.2. Biological catalysts
6.2.1. Aren't used up
6.3. Specific/ Unique
6.4. Hydrolyse polymers into monomers
6.5. Catabolic Reactions- Enzymes
6.5.1. Lactase
6.5.1.1. Lactose= Glucose + Galactose
6.5.1.1.1. Break down of milk sugar
6.5.2. Catalase
6.5.2.1. Hydrogen Peroxide= water + oxygen
6.5.2.1.1. H2O2 toxic byproduct of metabolism- must be removed
6.6. Anabolic Reaction- Enzymes
6.6.1. RUBISCO
6.6.1.1. RuBP + CO2= Glycerate Phosphate
6.6.1.1.1. Fixes CO2 from atmosphere in photosynthesis
6.6.2. ATPsynthase
6.6.2.1. ADP+Pi= ATP
6.6.2.1.1. Production of ATP for use in active processes
6.6.3. Glycogen Synthetase
6.6.3.1. Glucose = Glycogen
6.6.3.1.1. Converts glucose to a storage compound- glycogen
6.7. Activation Energy
6.7.1. Enzymes lower the activation energy
6.7.2. The difference in energy levels is the energy stored in the covalent bond between the monomers
6.8. Lock and key model
6.8.1. Enzymes have a specific active site that the substrate fits into perfectly due to its complementary shape and it breaks it down
6.9. Induced Fit model
6.9.1. The active site changes shape to fit more closely to hold in it and create a strain to breakdown the substrate
6.10. Measuring rate of reaction
6.10.1. Measure the concentration of product formed
6.10.2. Measure substrate used up after a fixed time interval
7. Proteins
7.1. Functions
7.1.1. Structure
7.1.2. Enzymes
7.1.3. Hormones
7.1.4. Antibodies
7.1.5. Protein receptors
7.1.5.1. E.g.
7.1.5.1.1. Insulin
7.1.6. Transport proteins
7.1.6.1. E.g.
7.1.6.1.1. Carrier proteins
7.1.7. Antigens
7.2. Amino Acids
7.2.1. Contains the elements carbon, hydrogen, oxygen and nitrogen
7.2.1.1. Sometimes sulphur
7.2.2. Simplest amino acid has the R- group of just hydrogen
7.2.2.1. Glycine
7.2.3. Some R-groups are charged
7.2.3.1. Polar
7.2.3.2. Hydrophilic
7.2.4. Some are R- groups are not charged
7.2.4.1. Non-polar
7.2.4.2. Hydrophobic
7.2.5. Formation of dipeptides and polypeptides
7.2.5.1. A condensation reaction occurs between the carboxylic acid group of one amino acid and the amine group of another to form a peptide bond
7.3. Fibrous Proteins
7.3.1. Forms long fibres
7.3.2. Has regular repetitive sequences of amino acids
7.3.3. Insoluble in water
7.3.4. Structural roles
7.3.5. E.g.
7.3.5.1. Collagen
7.3.5.1.1. Molecules cross link through covalent bonds
7.3.6. Triple helix structure
7.3.7. Every third amnio acids is glycine
7.3.8. Compact
7.3.9. 3 chains held together by hydrogen bonds
7.4. Globular Proteins
7.4.1. Compact ball like shape
7.4.2. Hydrophobic R- groups on amino acids
7.4.2.1. Inside
7.4.3. Hydrophilic R-groups
7.4.3.1. Outside
7.4.4. More water soluble than fibrous proteins
7.4.5. Metabolic role
7.4.6. Have a wide range of amino acid sequences
7.5. Structure Levels
7.5.1. Primary
7.5.1.1. Sequence of amino acids held together by peptide bonds- determine the secondary and tertiary structure
7.5.2. Secondary
7.5.2.1. The polypeptide chain coils to form an alpha helix or folds to form a beta pleated sheet
7.5.2.2. Held together by many weak hydrogen bonds
7.5.3. Tertiary
7.5.3.1. Further folding of the polypeptide chain with a more complex 3D shape
7.5.3.2. Hydrogen bonds
7.5.3.2.1. Weak bonds between the R-groups that are easily broken
7.5.3.3. Ionic bonds
7.5.3.3.1. Between positively and negatively charged R-groups of amino acids
7.5.3.4. Disulphide bonds
7.5.3.4.1. Formed between sulphurs in the R-group of the amino acid cysteine
7.5.3.5. Hydrophobic Interactions
7.5.3.5.1. Between non-polar R-groups that cluster together in the middle
7.5.4. Quaternary
7.5.4.1. Proteins made up of more than one polypeptide chain
7.5.4.2. Each chain contains a haem group which contain an Fe+ ion
8. Eukaryotic Cells
8.1. Nuclear Envelope
8.1.1. controls the exit and entry of materials in the nucleus
9. Nucleic Acids
9.1. Types of Nucliec acids
9.1.1. DNA
9.1.2. RNA
9.2. What Nucleic Acids consist of
9.2.1. Phosphate group
9.2.2. Pentose sugar
9.2.3. Nitrogen containing base
9.2.3.1. Adenine
9.2.3.2. Guanine
9.2.3.3. Thymine
9.2.3.4. Cytosine