2.

4 Proteins

Amino Acids

Amino acids are linked together by condensation to form polypeptides.

 Amino acids are joined to form polypeptides.

 By condensation reaction
 Involves the formation of a peptide bond between the amino acids
 Water is produced
 Enzymes might be needed
 Energy is released
 Examples: formation of insulin/ Hemoglobin

Drawing molecular diagrams to show the formation of a peptide bond.

Relationship between Amino Acids/ Polypeptides/ Proteins

 There are 20 different amino acids in polypeptides

 Amino acids link to form polypeptides by condensation reactions.
 Amino acids join by a peptide bond.
 Polypeptides are synthesized on ribosomes.
 The different “R” groups are what makes the amino acids different and allow the proteins to
form a wide array of structures and functions
 Some amino acids are polar, others are non-polar
 Amino acids can be linked together in any sequence giving a huge range of possible polypeptides.
 The amino acid sequence of polypeptides is coded for by genes
 Each 3 bases codes for 1 amino acid in a polypeptide
 most organisms use the same 20 amino acids in the same genetic code although there are some
exceptions.
 A protein may consist of a single polypeptide or more than one polypeptide linked together.
Example: Hemoglobin has 4 linked polypeptides, which are folded into a globular protein to
carry oxygen in the blood.
 The amino acid sequence determines the three-dimensional conformation of a protein.
 Living organisms synthesize many different proteins with a wide range of functions

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  There are 4 levels of proteins: primary, secondary, tertiary and quaternary

Q: What are the four levels of proteins?

Primary Structure:

Secondary Structure:

Tertiary Structure:

Ex. tRNA is a tertiary protein

Quaternary Structure:

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Every individual has a unique proteome

 A proteome is all of the different kinds of proteins produced by a genome, cell, tissue or
organism at a certain time.
 This is completed by extracting mixtures of proteins and using gel electrophoresis with
antibodies specific to those proteins with florescent markers
 Proteomes vary in different cells (different cells make different proteins) and at different times
within the same cell (cell activity varies)
 Proteomes vary between different individuals because of not only cell activity but slight
variations in amino acid sequences
 Within species there are strong similarities between proteomes

Living organisms synthesize many different proteins with a wide range of functions
(Functions of Proteins)

Function Example
Structural Collagen – strengthens bones, skin and tendons.
Movement Actin and Myosin – found in muscle fibers/
causes contraction of the muscle which results
in movement.
Transport Hemoglobin – transports oxygen throughout the
blood system
Defense/immunity Immunoglobulin – acts as an antibody for
defense against pathogens
Hormones Insulin – regulates blood glucose
enzymes pepsin – breaks down protein in the stomach to
polypeptides/dipeptides

Examples of the range of protein functions

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 Example of protein Function
Rubisco - Full name: ribulose bisphosphate carboxylase
- Catalyzes carbon fixation in the Calvin cycle in photosynthesis
- CO2 reacts with a 5-C sugar to form a 6-C compound.

Insulin - A hormone produced by β cells of the pancreas

- reduces blood glucose by stimulating muscle and liver cells to take up glucose from
the blood and convert it into glycogen.
- It binds reversibly to receptors in the cell membrane to stimulate the uptake.
Immunoglobulins - known as “antibodies”
- They are Y shaped proteins
- produced by B cells
- identify and neutralize foreign pathogens like bacteria and viruses
- they act as markers to identify these pathogens for destruction by large white
blood cells called Phagocytes
- each antibody is specific for a specific pathogen
Rhodopsin - a biological pigment in the photoreceptor cells of the retina
- consists of a retinal molecule surrounded by an opsin polypeptide
- When the retinal absorbs light through the eye, it changes it’s shape and the shape
of the opsin. This sends a nerve impulse through the optic nerve to the brain
- essential in low light
Collagen - main structure molecule in various connective tissues such as skin, blood vessels
and ligaments
- They are fibrous rope-like proteins made from 3 polypeptides
- Most abundant protein in the body (about ¼ of all the proteins)
Spider silk - spider silk consists of many different types with different functions
Eg. dragline silk is stronger than steel and tougher than Kevlar used in bulletproof
vests)
- used in the spokes of a web and when a spider suspends itself
- very extensible and resistant to breaking

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Denaturation of proteins by heat or by deviation of pH from the optimum. (studied in further detail in
enzyme section)

Temp

 Different proteins can tolerate different

temperatures.
 Most of the proteins in the humans work best
at body temperature 37.
 Heat causes proteins to denature because
vibrations caused by the KE break the
intermolecular bonds or interactions
 Heat alters 3D structure

PH

 Different pH’s away from a proteins optimal

pH can also cause denaturation
 Alkaline or acidic solutions can break the
ionic bonds between R groups causing the
protein to lose its 3D shape
 E.g Pepsin – Enzyme in the stomach works
best at about 1.5 pH but will denature as the
pH gets higher

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