Molecular biology is closely linked with biochemistry. Metabolism is the sum of all biochemical reactions in the body.
Organic molecules always contain carbon and hydrogen. Oxygen and nitrogen are also commonly found in 99% of living organisms.
Order of abundance: hydrogen > carbon > oxygen > nitrogen.
General formula: (CH2O)n
Carbohydrates are categorized depending on the number of carbon atoms they have. There are trioses (3C), pentoses (5C), and hexoses (6C).
The bond formed between two monosaccharides is known as a glycosidic bond.
Starch | Glycogen | Cellulose | |
---|---|---|---|
Monomers | α-glucose; amylose and amylopectin | α-glucose; amylose and amylopectin | β-glucose |
Bonding | amylose: 1,4 links \n amylopectin: 1,4 links and a branched 1,6 link | amylose: 1,4 links \n similar to amylopectin; 1,6 branched links | 1,4 linkage with every other β-glucose inverted; δ+ H atoms on hydroxyl (OH) groups form hydrogen bonds with δ- H atoms on other groups |
Function | energy reserves in plants | energy reserves in animals found in the liver and muscle cells | strengthening material of cell walls |
All lipids are organic molecules; non-polar and hydrophobic (insoluble) in water. They contain a lower proportion of oxygen compared to carbohydrates.
Lipids are made up of fatty acids and glycerol.
a fatty acid chain can be 15 to 17 carbon atoms long
unsaturated fatty acids contain carbon double bonds
glycerol is an alcohol with three hydroxyl (-OH) groups
Triglycerides are the most common form of lipids. They are insoluble in water but soluble in other organic solvents (e.g ethanol).
The bond forming a triglyceride is an ester bond that is formed from a condensation reaction. It is broken apart by a hydrolysis reaction.
Lipids make excellent energy reserves because of the richness in carbon-hydrogen bonds
Fat is stored below the dermis (skin) and around the kidneys. Fat is responsible for;
Phospholipids are similar to triglycerides. However, one fatty acid chain is replaced by a phosphate group.
Proteins are important in cells as they are responsible for:
There are 20 different amino acids found in all living organisms. These can be differentiated by their R group.
A dipeptide/polypeptide is made through a condensation reaction to form a peptide bond between two amino acids. It is broken down by a hydrolysis reaction.
Proteins have four structures: primary (1°), secondary (2°), tertiary (3°), and quaternary (4°).
Some proteins can have prosthetic groups as part of their structure. These are non-proteins combined with proteins as it is required for their function.
There are globular and fibrous proteins:
Features | Globular | Fibrous |
---|---|---|
Shape | roughly spherical/circular | long strands |
Amino acid sequence | irregular; wide range of R groups used | repetitive; limited range of R groups used |
Function | physiological \n metabolic | structural |
Examples | haemoglobin, enzymes, insulin | collagen, keratin, myosin |
Solubility | (generally) soluble in water | (generally) insoluble in water |
Features | Haemoglobin | Collagen |
---|---|---|
Number of polypeptide chains | 4 (2 α-globin, 2 β-globin) | 3 (triple helix) |
Shape | spherical/round | long, thin |
Function | transport of oxygen; binds to haem group | in connective tissue e.g tendons, skin |
Amino acid variation | variable | repetitive; every third amino acid is glycine |
Prosthetic group? | present; haem group with iron (II) ion | not present |
Solubility | soluble in water | insoluble in water |
Water is dipole as it has a negative region (oxygen) and a positive (hydrogen) region. This makes water polar.
Properties of water include:
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