BIOL130 Lecture 2: Unit 2
Macromolecules
Macromolecules are large, organized molecules which come together to perform certain functions. They
are made through polymerisation
Biological macro molecules are what provide for the structures and properties of the cells (carry out the
activities)
There are four groups of macromolecules there are:
• Carbohydrates (polysaccharides)
• Lipids
• Proteins
• Nucleic acids
The difference between thee is that ideally, their monomers are different.
The general theme for generating macromolecules follows the chain and reactions known as
condensation and hydrolysis. Condensations is the idea of taking a water molecule of the compound, in
order for the compound to search for new bonds to match with the molecules of H or OH (depending on
what came off during the condensation)
Hydrolysis on the other hand is the addition of a water molecule for the purose of breaking the bonds of
a macromolecule into two different components.
What are functions of proteins?
• There are very specialised and due to this, they hold many important tasks within our bodies
cellular and molecular makeup. One of these is that there are enzymes that are made up
proteins. Enzymes are a type of catalyst that allows for the speed time of many reactions
without our bodily systems to go faster. It is important to note that without enzymes, our bodies
would not functions as many reactions would be too slow
• Proteins, due to their characteristics also allow for fluidity within the call, in specific, the cell
membrane.
• They also provide as a support for many of our components including the cytoskeleton and the
hairs of our bodies.
• Messenger proteins which allow for signaling around the body
• They also allow for the movement of the cell itself. Some ways it does this include the flagella
(protein based)
• And finally, proteins also allow for defence within the cell (antibiotics)
Proteins are commonly known as polymers. This is because they are made up from two or more amino
acids which come together to form these specialised molecules. There are 20 amino acid monomers to
pick from for the protein in order to perform the special tasks that it does.
From the name itself we can understand that amino acids are made up of two components: an amino
group and a carboxylic acid. There is also a central carbon, known as the alpha carbon.
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The R group of each amino acid is different. There are 2 forms of this monomer and these are L and D
isomers. The difference between the two is that the L is the reverse of the D shaped one. We most
commonly find the L shaped.
Amino acid side chains are generalised into two different classes, one is non polar and the other is polar.
Polar is further separated into uncharged and charged.
Non polar side chains are essentially hydrophobic R groups, these are essentially uncharged sets of
oleules at the eds of the hai, hih allo the aio aid to repel HOs attratie fores. The H
atoms are already linked onto usually C atom which allow the attraction to be negated.
Uncharged polar side chains are side chains that have already bonded atoms together, but the bonds
are potentially not strong enough to hold intact when the presence of H atoms becomes apparent (H
bonds are strong)
Charged polar side chains are side chains that are very soluble in water
There is a special type of bond between these amino acids which holds them together. This is known as
the peptide bond. Essentially the chains of these are linear
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The main factors which allow this peptide bond to form is the hydrolysis and condensation of the
molecule
Sickle cell anemia is a disease where red blood cells are abnormally shaped, caused by single point
mutation which results in the substitution of one amino acid in the hemoglobin protein chain.
Depending on how hydrophobic/ hydrophilic the amino acid is, change the structure of the cell
completely.
There are several different level of protein structures. In the primary sequence is where all the
information is coded
There are three levels if structure that organize the folding of the amino acids in the polypeptide.
• Primary is the linear sequence of the amino acid
• Secondary is the folding of the primary sequence into the amino acid specific sequences
• Tertiary is the interactive step, where different amino acids interact with each other in their
folded states to create a 3 dimensional globular shape
• Quaternary is when two or more polypeptides interact to form the functional protein
Specific to secondary structure, there are two different forms of the structure which each provide
different attributes to the amino acid group. The Helices is a parallel pleated sheet, whereas the beta
strand is the anti-parallel pleated sheets.
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Document Summary
Macromolecules are large, organized molecules which come together to perform certain functions. Biological macro molecules are what provide for the structures and properties of the cells (carry out the activities) There are four groups of macromolecules there are: The difference between thee is that ideally, their monomers are different. The general theme for generating macromolecules follows the chain and reactions known as condensation and hydrolysis. Condensations is the idea of taking a water molecule of the compound, in order for the compound to search for new bonds to match with the molecules of h or oh (depending on what came off during the condensation) Hydrolysis on the other hand is the addition of a water molecule for the purose of breaking the bonds of a macromolecule into two different components. What are functions of proteins: there are very specialised and due to this, they hold many important tasks within our bodies cellular and molecular makeup.
