CHEMISTRY

15. Option B: Human Biochemistry

Energy Requirements
E = M(KG) * 4.18 * T (C)

Proteins
Proteins form an essential part of a healthy diet and perform many key functions
in the body.
Sourced from foods such as meat, fish, cheese, eggs and nuts.
Proteins act as :
Biological catalysts (enzymes)
Transporters for haemoglobin in the blood
Structure (hair, nails)
Source of energy
Hormones

2- Amino Acids
Proteins are large macromolecular made up of chains of 2-amino acids.
Approximately 20 amino acids occur naturally.
GENERAL FORMULA: H2NCHRCOOH
In aqueous solution:
At low pH the amine group will be protonated
At high pH the carboxylic acid group loses a proton (COO-)
Isoelectric Point The pH value where the amino acid will exist as a zwitterion
2- amino acids function as good buffers, as they can combine with protons or
hydroxide ions, maintaining pH of solutions.
Two 2-amino acids will condense to form a dipeptide (elimination with water).
O H
|| |
--C-N--

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Above shows a peptide bond that occurs in a dipeptide, after condensation
polymerization. The products are known as polypeptides.

Structure of Proteins
Proteins are made up from fixed number of amino acid residues connected.
Prefixes leu- his ala- val- ala ser COOH
This is known as the primary structure of proteins, refers to the amino acid
residues that are connected to create the full chain.
Secondary Structure This describes the way in which the chains of amino
acids fold themselves.
Alpha helix (intramolecular hydrogen bomding)
Beta pleated sheet (intramolecular hydrogen bonding between polypeptide
chains)

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Tertiary Structure Overall folding of chains by interactions to give a threedimensional shape. Interactions occur due to the hydrogen bonding, Van der
Waals attraction between non-polar side groups and ionic attractions between
polar groups.
(DISULFIDE BRIDGE CREATED WHEN TWO CYTOSINE GROUPS UNDERGO
ENZYME CATALYSED OXIDATION)
Separate polypeptide chains interact to create a more complex structure known
as Quaternary structure of proteins.

Analysis of Proteins
Proteins must be hydrolysed by dilute HCL in order to break the protein down
into amino acid groups.
Chromatography or electrophoresis
Developed by spraying the amino acids with ninhydrin, an organic dye that
colors the amino acids, so that the retention factor Rf of the spots can be
determined and compared with known values. (CHROMATOGRAPHY)
Proteins are placed in a magnetic field- positive R-groups will be attracted to
the negative pole of the magnet, while negative R-groups will tend to move
towards the positive pole.
The position where the individual amino acids stop is indicative of their
charge. This reveals the isoelectric point, and consequently the R-group of
the amino acid.
pH can be used to separate proteins. They re placed in a pH gradient. Amino
acids travel to where their net charge is zero. Given the position in which
they stop, the amino acid can be identified.

Carbohydrates
Carbohydrates are a principal source of energy for the human body.
The human body uses carbohydrates to store energy in the form of glycogen
(animal starch).
Carbohydrates are a precursor for components of nucleic acids and the
biosynthesis of proteins.

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Dietary fibre is also a carbohydrate, in forms that the human body cannot break
down. It is typically plant material, which cannot be broken down in the
digestive tract.
It provides roughage for good bowel movements.
Deficiency leads to IBS, constipation, obesity, and diabetes.
Examples: cellulose, lignin, pectin

Monosaccharides
Monosaccharides have empirical formula CH2O and contain a carbonyl and at
least 2 hydroxyl groups.
Commonly found as glucose, D-glucose (naturally occurring)
D- Glucose has a straight chain formula, as well as a ring structure which has two
forms known as alpha and beta D-Glucose.
The difference is the OH on the first carbon atom group is inverted.

Polysaccharides
Sugars can condense in the presence of proper enzymes to form polysaccharides.
The link between the two sugars is known as a glycosidic link.
Glycogen, stored in the liver can break down into glucose for energy when it is
needed.
Polysaccharides are precursors for other biologically important molecules.
An alpha and beta sample of D-Glucose and D-Fructose can be joined using a
glycosidic link, a link between C-1 of the alpha and the C2 of the the beta sample.
This glycosidic reaction will create sucrose, common table sugar.
Starch is created through chains of alpha glucose, in the form of amylose and
amylopectin. Amylose contains alpha 1,4 bonds. Amylopectin contains
i.e. monosaccharides are used to make other molecules like glycerol and fatty acids and
some amino acids. -Cellulose-structural material in plants

Lipids
Lipids are organic molecular with long hydrocarbon chains that are soluble in
non-polar solvents

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Unsaturated (one or more double bond) Saturated (no double bonds)
The extent of unsaturation of a lipid can be found through its Iodine Number
Functions : Energy source, insulation, Cell membrane(phospholipids)

Cholesterol
Cholesterols have the characteristic four-ring structure possessed by all
steroids.
Formed in the liver, found in all tissues.
Transported by lipoproteins. LDL transport cholesterol to arteries where they
line the walls, leading to cardiovascular disease. LDL (saturated fats).
HDL, can remove cholesterol from arteries and transport it back to the liver.

Vitamins
Vitamins play a key role in metabolism and vital body functions.
All of the bodys biochemical reactions require enzymes and co-enzymes,
vitamins functions as these co-enzymes.
Vitamin B and C are soluble in water
Vitamin A and D are stored in fat tissue, insoluble in water.
Vitamin Functions
Vitamin A (retinol) at night, light shining on the eye strikes a receptor,
rhodopsin which sends an impulse to the brain. Vitamin A helps produce
rhodopsin.
Deficiency = night blindness

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Vitamin D (calciferol) Important in production of a hormone involved in the
metabolism of calcium. Acts as a hormone allowing the intestines to absorb
calcium from food.
Deficiency = Rickets, Brittle bones
Vitamin C (ascorbic acid) Essential in the formation of connective
tissue(collagen). Works as a reducing agent to form amino acid of collagen.
Deficiency = scurvy (connective tissue breaks down).

Hormones
Controlled by the pituitary gland, secreted by endocrine glands.
Adrenalin
Synthesized from Thyrosine, causes blood to be sent to areas of more active
circulation.
Causes increase in heart rate, stimulated respiration, causes breakdown of
glycogen to glucose, raises levels of blood sugar.
Thyroxine
Produced by the thyroid gland, stimulates growth and metabolism.
Deficiency can result in hypothyroidism, characterized by lethargy and dry skin.
Over-consumption leads to hyperthyroidism, anxiety, weight loss, intolerance to
heat etc.
Insulin
Made up of two polypeptide chains, held by disulfide bonds. Created in the
pancreas and regulates cellular intake of glucose from the blood. Secreted in
response to a rise in blood sugar .
In diabetics insulin levels are low, and glucose in not transferred sufficiently
from bloodstream to tissue . Hyperglycemia results in thirst, weight loss, coma.
Sex Hormones
Female : Pituitary hormones are secreted at puberty. Estrogen results in an
increase of secretion of these hormones resulting in follicles and ovulation

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Male : Testoterone secreted by testes and adrenal glands. During puberty
pituitary gland secretes ABP which results in typical male puberty changes.

Oral Contraceptives
Pill contains estrogen and progesterone. Excess of these hormones prevents
ovulation, thus reducing risk of pregnancy. Lowered levels of LH and FSH stops
the development of endometrium lining

Enzymes
Enzymes are protein molecule catalyse biological reactions.
Inhibitors are substances that decrease the rate of enzyme-catalysed reactions.
Competitive inhibitors resemble the substrate in shape but cannot react, they
slow down reactions because they occupy the active site on the enzyme.
Non competitive inhibitors also bind to the enzyme but not on the active site.
Enzyme activity is affected by:

Temperature (maximum Ea up to a cap).

pH (charges on amino acid residues change at different pH values)
Heavy Metals can poison enzymes by reacting with SH groups and
altering the tertiary structure.

Nucleic Acids
Nucleic acids are natural polymers made up of nucleotides . All cells in the
human body(bar RBCs) DNA.
A nucleotide of DNA contains deoxyribose (pentose sugar), covalently bonded to
a phosphate group and one of four nitrogen-containing bases: adenine, guanine,
cytosine or thymine (A, G, C ,T)
Nucleotides of RNA contain a different pentose sugar (ribose), but contains a
phosphate group and four nitrogen bases, A, G, T and URACIL (U).
When cells divide, genetic information has to be replicated.
The genetic information is stored in chromosomes.
A chromosome is a long sequence of DNA
DNA in the cell starts to unzip and hydrogen bonds between bases are broken,

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DNA Profiling
Helps to solve crimes using DNA in blood, semen, hair or saliva.
The specimen is broken down using restriction enzymes to smaller fragments
known as minisatellites.
The fragments are separated into bands using electrophoresis gel.
The fragments can create a characteristic fingerprint, used to determine genetic
matches.

Respiration
In the body 1 mol of glucose is broken down in a prcess known as glycolysis to 2
mol of pyruvate. Glycolysis produces energy storing it olecules of ATP.
The pyruvate may break down aerobically or anaerobically.

C6H12O6 + O2 2 C2H4O3 + 2H2O

Then
2C3H4O3 + 5O2 6CO2 + 4H2O
overall
C6H12O6 + 6O2 6CO2 + 6H2O