fructose

Classification = Simple carbohydrates and Complex carbohydrates

Carbohydrates = Sugar + Starches 'CHO' = ex. Sugar Starches Cellulose palmitic acid and
stearic acid
Lipids = Fats + Oil 'CHO' = ex. Saturated + Unsaturated Fats Oils Mono = Oleic acid
Poly = Linoleic acid
Nucleic Acid = Nucleotide = Nucleoside + Phosphoric Acid 'CHONP' = ex. DNA RNA N2
Growth and Maintenance. Causes Biochemical Reactions. Acts as a Messenger. Some proteins are
Bases Pentose Sugar hormones, which are chemical messengers required for the structure, function, and regulation of the
body's tissuesandorgans.
Protein = Amino Acid 'CHON' = ex. Amino acid liked by Peptide bond
Proteins are very large molecules composed of basic units called amino acids
Simple Protein = Albumin,Globulin,Histones,Globins,Protamines,Glutelins. Only composed of amino acid
only
aka complex
Conjugated Protein = Nucleoproteins, Lipoproteins, Metalloprotein, Chromoprotein,
Glycoproteins, Phosphoproteins Composed of amino acid and non protein components like lipid, carbs
Derived Primary = Proteans,Metaproteins,Coagulated Proteins Myocardial infaction
Derived Secondary = Proteoses,peptones,polypeptides,peptides
LDH1 MB isoform of
Creatine kinase
Nucleotides consist of nucleosides + phosphates. Ex. DNA RNA
Nucleoside nitrogen base and pentose sugar The main function of carbohydrates is to provide energy and
food to the body and to the nervous system.
N2 Base are aromatic heterocyclic structure divided into two groups:
1. Purines: Adenine, Guanine Disulfide bond Stabilises tertiary H-bond
2. Pyrimidines: Cytosine,Thymine, Uracil vanderwall force electrostatic force
attraction
Chargaff Rule A + G = T + C uracil which is only found in RNA
sum of purine bases is equal to the sum of pyrimidine bases

Amino Acid -Building blocks of proteins -Have amino and carboxyl group -Classification...
1.Non Polar = Glycine, Alanine, Proline, Valine, Leucine, Methionine
2.Polar = Serine, Threonine, Cysteine, (-)Asparagine, (-)Glutamine, (+)Lysine,(+)Arginine

Essential AA
Amino acid that can not be synthesised by body. Ex. histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, threonine, tryptophan, and valine
WHY ? = {because the human body lacks the metabolic pathways which required to
synthesize these amino acids}

Non Essential AA
Amino acid that can be synthesised by body. Ex. alanine, arginine, asparagine, aspartic
acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine

ZwitterIon
 It is a molecule that has a positive charge on one atom and negative charge on another
atom that means the net charge on it is zero And also have isoelectric pH.

Peptide is form when >2 AA join together

Peptide bond is a bond between the carboxyl group of one amino acid and the amino
group of another amino acid. It link amino acids together.

Primary Protein Structure = Sequence of a chain of AA

Secondary Protein Structure = Sequence of polypeptide chain due to formation of
hydrogen bonds between components of peptide bonds.
Tertiary Protein Structure = three - dimensional shape that results from the attractive
forces between amino acid side chains (R groups) that are widely separated from each
other within the chain.
Quaternary Protein Structure = Occurs when >2 protein units combines ex. Haemoglobin.

α-Helix is coiled secondary structural arrangement of many proteins consisting of a single

chain of amino acids stabilised by hydrogen bond between CO and NH groups of
neighbouring chains.
β-Pleated sheet is a type of secondary structure of a protein that consists of various beta
strands linked by hydrogen bonds between CO and NH groups of neighbouring chains.

DNA Secondary Structure given by james wateson and francis crisk.

DNA molecule consists of two chains, which form right-handed helix, where both chains
are coiled around the common axis. Each strand has an opposite polarity to the other and
are antiparallel
connecting genetic information in DNA and the amino acid sequence of proteins. it contains codons that are complementary to
the sequence of nucleotides on template strand
mRNA = Also called messenger RNA. Carry the information from the DNA in the nucleus
of the cell to the cytoplasm where the proteins are made.
rRNA = forms part of the protein synthesizing organelle i.e. ribosome and that is
exported to the cytoplasm to help in translation of information in mRNA into protein
codon sequence of the mRNA is translated accurately into amino acid sequence in proteins
tRNA = helps in decoding a messenger RNA sequence into a protein
It carries the amino acid to be added in the peptide chain and from getting info from codon from mRNA molecule.

Denaturation of DNA is caused by:

Biological role of albumin is to produce
-sharp pH change to acidic or alkaline side; and control oncotic pressure and is the
-heating of DNA solution main transporter plasma protein

Lactate dehydrogenase (LDH) Albumin is the most common protein found in blood plasma. It helps
to ensure blood stays in arteries and veins, and helps carry
hormones, vitamins, and enzymes
pressure in the circulatory system which encourages water to cross the barrier of the capillaries and enter the circulatory system
Is an enzyme found in almost all body tissues. It plays an important role in cellular
respiration, the process by which glucose (sugar) from food is converted into usable
energy for our cells. Effect of Temp on Enzyme reaction rate is if the
Temp increases it increses the speed of reaction
In myocardial infarction LDH1(H4) increases. but after optimum temperature it get slowed and
get denatured. lower temperatures decrease the
rate of an enzyme reaction
Aminotransferases or transaminases are a group of enzymes that catalyze the
interconversion of amino acids and oxoacids by transfer of amino groups. (AST) Serum
aspartate transaminase is mainly found in the liver, cardiac muscle, and other tissues and
(ALT) serum alanine transaminase is predominantly found in the liver.
a substance produced by a living organism which acts as a catalyst which help
ENZYMES in fastening of the reaction (aka autocatalyst)
1 OXIDOREDUCTASES: catalyze oxidation/reduction reactions
2 TRANSFERASES: transfer a functional grout (e.g. a methyl or phosphate group)
3 HYDROLASES: catalyze the hydrolysis of various bonds
4 LYASES: cleave various bonds by means other than hydrolysis and oxidation
5 ISOMERASES : catalyze isomerisation changes within a single molecule
6 LIGASES: join two molecules with covalent bonds.

Specific properties of organic catalysts, or differences between enzymes and inorganic

catalysts: Globulins are a group of proteins in your blood. They are made in
your liver by your immune system. Globulins play an important role
• High efficiency of action. in liver function, blood clotting, and fighting infection. There are four
main types of globulins. They are called alpha 1, alpha 2, beta, and
• High specificity of action. gamma.
• They act under physiological conditions (as so called soft conditions):
37°C- temperature of body; physiological pH; normal pressure.
• Cooperative effect. Histone = Basic in nature + Found in
dna + provides structural support for
chromosome
• The oriental effect is typical for enzymes.
• They practically do not form side products.
• Enzymes are regulated

Enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity.
Artificial inhibitors are often used as drugs, but
can also be insecticides such as malathion, herbicides such as glyphosate,
or disinfectants such as triclosan.
Catabolism = the breakdown of complex molecules in living organisms to form
simpler ones
Kreb 12 atp
gluconeogenesis = metabolic pathway that results in the generation of glucose
from certain non-carbohydrate carbon substrate