Proteins

SL CONTENT
B1.2.1—Generalized structure of an amino acid
Proteins are long chains of recurring monomers called amino acids. They are the building
blocks of proteins.
Amino acids all share a common basic structure, with a central carbon atom bound to:
■ An amine group (NH2)
■ A carboxylic acid group (COOH)
■ A hydrogen atom (H)
■ A variable side chain (R)

Each of the 20 amino acids has a different R-group. R-groups can be non-polar or polar,
linear or in ringed form, providing each amino acid with distinct chemical and physical
properties.
- Central carbon is the alpha carbon, the alpha carbon has 4 single covalent bonds to
4 other atoms, (Hydrogen, Nitrogen, R group and carbon)
- The carboxyl (-COOH) group is acidic as it can donate a proton, and the amine group
is basic as it can accept one, so amino acids are amphiprotic.
- An amphiprotic substance is a proton-bearing molecule that is capable of
donating its proton as well as accepting an additional proton. For a molecule
to be amphiprotic, it must satisfy the following: It must contain a hydrogen
atom that can be released as a proton.

B1.2.2—Condensation reactions forming dipeptides and longer chains of amino acids

Amino acids can be covalently joined together in a condensation reaction to form a dipeptide
and water
The covalent bond between the amino acids is called a peptide bond and, for this reason,
long chains of covalently bonded amino acids are called polypeptides
Polypeptide chains can be broken down via hydrolysis reactions, which requires water to
reverse the process.
 - Amino acids join together through a condensation reaction. A peptide bond is formed
when the carboxyl group (–COOH) of one amino acid reacts with the amino group (–
NH2) of another amino acid to form a dipeptide. A molecule of water (H2O) is
released as a byproduct. The peptide bond formed is a type of covalent bond and,
therefore, is very stable.

There is a single bond between C and N. This is dipeptide above.

- To form a dipeptide, two amino acids are linked by a condensation reaction.
Polypeptides can contain any number of amino acids, though chains of less than 20
amino acids are usually referred to as oligopeptides. Polypeptides are the main
components of proteins.
- Polypeptide - A chain of amino acids that is linked together by peptide bonds.
 - Peptide bond - The bond between the Nitrogen in the amine group and Carbon in
the carboxyl group that links 2 amino acids together.

A dipeptide can be separated via a hydrolysis reaction, where water is added to separate the
2 amino acids.

B1.2.3—Dietary requirements for amino acids

Amino acids can be classified as either essential or non-essential.
- Essential amino acids are the amino acids that your body cannot produce and
therefore you must obtain them from the food that you eat. Essential amino acids are
necessary for proper growth, maintenance and repair of the body’s tissues and
organs.
- Non-essential amino acids can be produced by the body from other amino acids or
by the breakdown of proteins. Non-essential amino acids, although not required in
the diet, still have important functions in the body. It is important to consume a
balanced diet that includes the appropriate combination of protein sources to ensure
the body’s needs are met.
- A non essential amino acid = can be synthesised by an animal using
metabolic pathways that transform one amino acid into another. (E.g.
Phenylalanine is essential as it is used to synthesise tyrosine)
- Vegan diets - Vegan diets can provide all the essential amino acids necessary for a
healthy diet through plant-based protein sources such as beans, lentils, nuts, seeds
 and tofu. However, if following a vegan diet, it is necessary to ensure that adequate
amounts of these protein sources are consumed for optimal health.

Foods vary in their amino acid content. Animal-based diets have a balance of amino acids
that is similar to what is needed for humans. However, plant-based diets have a different
balance, as some are deficient in specific amino acids.
- Protein malnutrition may lead to a decrease in immunity and mental alertness,
slowed growth and fatigue.
Infinite variety of possible peptide chains
- Ribosomes link amino acids together one at a time until a polypeptide is fully
formed. Ribosomes do not make random sequences of amino acids. Rather, they
receive specific instructions in the form of a universal, genetic code.
- Ribosomes - A ribosome is the cellular machinery responsible for making
proteins. There are many ribosomes in each cell, each made up of two
subunits.
- Genetic code - A set of rules that specifies how information stored in DNA is
translated into the sequence of amino acids that make up proteins.
- The genetic code provides the instructions for the synthesis of proteins through the
processes of transcription and translation.
- Transcription - Process by which the genetic information encoded in DNA is
copied into RNA.
- Translation - Process by which ribosomes use the genetic information
carried by mRNA to synthesise proteins.
- The genetic code is composed of codons, which are groups of three nucleotides that
specify the type of amino acid or stop signal required. There are 64 different codons
in total, but only 20 amino acids, so the genetic code is said to be degenerate. This
means that some amino acids are coded for by multiple codons, which allows for the
possibility of silent mutations.
- Silent mutations - are where a change in the DNA sequence does not result
in a change in the amino acid sequence of the protein.
- Codons - A set of three adjacent nucleotides in DNA or mRNA that code for a
particular amino acid.
- Degenerate - Refers to the redundancy in the genetic code, which allows for
multiple codons to code for the same amino acid.
- set of 3 adjacent nucleotide codes for the 20 amino acids, so the genetic code is
degenerate, referring to the redundancy in the genetic code, which allows for multiple
codons to code for the same amino acid. The number of possible amino acid
sequences can be calculated for a polypeptide of “n” amino acids: 2 0n
- So the infinite variety of possible peptide chains arises from the ability to
combine the 20 different amino acids in any sequence.
- Based on the three letters that are present in a codon, a codon table can be used to
deduce which amino acid the codon codes for.
 - For example, if the codon is GCU, you will use the table to see where the first letter is
G, the second letter is C and the third letter is U. In this case, you will find that GCU
codes for the amino acid alanine.

- The number of possible sequences is effectively infinite. But only extremely small
proportions are made by an organism. This is the organism’s proteome. The genetic
code, combined with the ability to generate diverse combinations of amino acids, is
what makes the complexity and diversity of life possible.
- Proteome - the totality of proteins expressed within a cell, tissue or organism
at a certain time
Examples of polypeptides:
- Beta-endorphin is a natural pain killer secreted by the pituitary gland that is a
polypeptide of 31 amino acids
- Insulin is a small protein that contains two short polypeptides, one with 21 and the
other with 30 amino acids
- Alpha-amylase is the enzyme in saliva that starts the digestion of starch. It is a single
polypeptide with 496 amino acids, with one chloride ion and one calcium ion
associated
- Titan is the largest polypeptide discovered so far. It is a polypeptide of 34,350 amino
acids.
 - The 20 different amino acids
-

Effect of pH and temperature on protein structure

- The structure of proteins is vital for their biological function and any changes to their
structure can result in a loss of activity.
- The three-dimensional conformation of proteins is stabilised by bonds or interactions
between the R groups of amino acids within the molecule. Most of these bonds and
interactions are relatively weak and can be disrupted or broken. This change in
conformation is denaturation.
- Denaturation - A process in which the structure of a protein is altered, causing it
to lose function, usually permanently.
- When proteins denature, its 3D shape is disrupted. It is a structural change in a
protein that results in the loss (usually permanent) of its biological properties. When a
protein is denatured the structural change is usually irreversible. These irreversible
changes may lead to the loss of biological properties and may lead to inactivity.
- Denatured proteins have a loss of secondary and tertiary folding compared
to active (functional) proteins. Both have no change in the primary
structure.
Denaturation is a structural change in a protein that results in the loss (usually permanent) of
its biological properties
■ Because the way a protein folds determines its function, any change or abrogation of
the tertiary structure will alter its activity

Denaturation of proteins can usually be caused by two key conditions – temperature and pH

- Factors:
- Extreme changes in pH(very high or very low[very basic or very acidic]) can
affect protein solubility and shape by altering the protein’s charge. This can
lead to irreversible changes in protein structure, causing inactivity. For
example, the enzyme pepsin requires an acidic environment to function, while
an alkaline environment will render it inactive.
- Soluble proteins often become insoluble and form a precipitate. This is
due to the hydrophobic R groups in the centre of the molecule being
exposed to water by the change of conformation.
1. Amino acids are zwitterions, neutral molecules possessing
both negatively (COO–) and positively (NH3+) charged regions
2. When the positive and negative charges on R-groups are
changed, it breaks ionic bonds within the protein or causes
new ionic bonds to form, resulting in denaturation
3. Changing the pH will alter the charge of the protein, which in
turn will alter protein solubility and overall shape.
-
 - High temperatures can break the weak hydrogen bonds holding the
protein structure together, causing the protein to unfold and lose
function. Most human proteins function optimally at body temperature
(~37 °C). Some organisms that live in extreme high-temperature
environments have proteins that can only function at higher temperatures.
Low temperatures can also affect protein structure, but to a lesser extent than
high temperatures.
Other ways of denaturation include exposure to chemicals (e.g. solvents and cleaners) or
vigorous shaking.
The amino acid sequence of polypeptides is coded for by genes
A gene is a sequence of DNA which encodes a polypeptide sequence
A gene sequence is converted into a polypeptide sequence via two processes:
■ Transcription – making an mRNA transcript based on a DNA template (occurs within
the nucleus)
■ Translation – using the instructions of the mRNA transcript to link amino acids
together (occurs at the ribosome)

Typically, one gene will code for one polypeptide – however there are exceptions to this rule:
■ Genes may be alternatively spliced to generate multiple polypeptide variants
■ Genes encoding tRNA sequences are transcribed but never translated
■ Genes may be mutated (their base sequence is changed) and consequently produce
an alternative polypeptide sequence
HL content

Chemical diversity in the R-groups of amino acids as a basis for the immense
diversity in protein form and function
While amine groups and carboxyl groups are used to link amino acids together, the R-group
is what gives each amino acid its unique characteristics. The R-groups of the amino
acids present in a polypeptide determine the properties of the assembled polypeptides.
- R-groups can be hydrophobic or hydrophilic.
- Hydrophobic R-groups are non-polar and tend to repel water molecules. Hydrophilic
R-groups are polar or charged, acidic or basic, and tend to attract water molecules.
- Polar R-groups contain partial charges that interact with water molecules, while
charged R groups can be either positively charged (basic) or negatively charged
 (acidic).

9 R-groups are hydrophobic with 11 R-groups are hydrophilic

0 to 9 carbon atoms

3 R-groups 6 R-groups do 4 hydrophilic R- 7 R-groups can become charged

contain rings not contain rings groups are polar
but never 4 R-groups act as an acid 3 R-groups act as a base
charged by giving up a proton and by accepting a proton and
becoming “-” charged becoming “+” charged
20 amino acids that ribosomes use to make polypeptides are varied in the chemical nature
of their R-groups. This broad diversity allows living organisms to make and use a wide
range of proteins.

If the R-group does not have an oxygen atom, it is a non-polar hydrocarbon. The amino
acid will be hydrophobic and will fold into the interior of the protein.

If the R-group has an oxygen atom, it is hydrophilic. If it does not have a charge, the
amino acid is polar and will fold into the exterior of the protein.

If the R-group has an oxygen atom and it has a charge, the amino acid is an ion (has fully
gained or lost an electron). These amino acids will be hydrophilic and will be capable of
forming ionic bonds with oppositely charged ionic amino acids. It will most likely fold into the
exterior of the protein.

Hydrophobic R groups will cause the protein to be hydrophobic and fold into the protein, so it
is away from water and attracted to other hydrophobic molecules

Hydrophilic R groups will cause the protein to be hydrophilic and fold into the exterior of the
protein as it is attracted to the water outside of the protein.

The impact of the primary structure on the conformation of the proteins

Primary structure - Structure of a protein that refers to the specific sequence of amino
acids that are joined together to form a polypeptide chain.
- The primary structure is the linear sequence of amino acids in a polypeptide. The
backbone of a polypeptide is a repeating sequence of atoms linked together by
covalent bonds. (-C-C-N-C-C-N and so on). The bond angles are all tetrahedral,
and there can be rotation about the bonds between the alpha carbon atoms and
adjacent nitrogen and carbon atoms. This allows polypeptides to fold into almost any
3D shape.
- The unique sequence of amino acids determines how the polypeptide chain will fold,
ultimately leading to the three-dimensional structure of the protein. This means that
the precise position of each amino acid within the protein structure is critical in
determining its shape.
 -

- The three-dimensional arrangement of atoms in a polypeptide or protein is its

conformation. Most polypeptides self-assemble into a specific conformation
determined by the sequence of amino acids and their R-groups. The precise position
of each amino acid within the protein structure is critical in determining its shape.

Pleating and coiling of the secondary structure of proteins

Secondary structure - Structure of a protein that refers to the local folding patterns that
occur within the polypeptide chain.
The 2 common secondary structures are:
- Alpha helix structure - A type of secondary protein structure that forms coils or helix
with a right-hand twist.
- The polypeptide would wound/spiral into a helical shape with a right-hand
twist, held in place by the hydrogen bonds between adjacent turns of the
helix.
- Beta pleated sheets - A type of secondary protein structure that forms pleats.
- Two or more sections of polypeptide are arranged in parallel with hydrogen
bonds between them. The sections of polypeptide run in opposite directions,
forming a sheet that is pleated because of the tetrahedral bond angles.

- The formation of alpha helices and beta-pleated sheets is facilitated by the ability of
the polypeptide chain to fold into coils and pleats, respectively. This is achieved
through hydrogen bonding between the carboxyl group of one amino acid and the
amino group of another amino acid in a different part of the polypeptide chain.
- At regular intervals along a polypeptide chain, there are C=O and N-H
groups. They are what remains of carboxyl and amine groups after they have
been used to make peptide bonds.
- Both C=O and N-H are polar, with the oxygen having a slight negative
charge and the hydrogen having a slight positive charge. Due to this
polarity, hydrogen bonds can form between these groups.
- In an alpha helix, the hydrogen bond forms between the amine hydrogen of one
amino acid and the carboxyl oxygen of another amino acid that is four residues away
in the sequence. This repeated pattern of hydrogen bonding allows the polypeptide
chain to coil and form the characteristic helical structure.
- In contrast, beta-pleated sheets form when sections of the polypeptide chain run
parallel to each other, and hydrogen bonds form between adjacent strands. These
hydrogen bonds create a pleated sheet-like structure, with the individual strands
forming the flat surface of the sheet
These hydrogen bonds occur in regular positions and help to stabilise and aid in the
formation of the secondary structure. Although a hydrogen bond on its own is considered to
be a weak form of bonding, collectively, hydrogen bonds are strong enough to hold the
conformation of the protein.
Dependence of the tertiary structure on hydrogen bonds, ionic bonds, disulfide
covalent bonds, and hydrophobic interactions
Tertiary structure - Structure that gives rise to the overall three-dimensional shape of the
protein.
- Tertiary structure is the folding of a whole polypeptide chain(so tertiary structures
have a polypeptide backbone) into a three-dimensional structure. This structure is
stabilised by the interactions between the R-groups. Which may include the formation
of hydrogen bonds, ionic bonds, disulfide covalent bonds and hydrophobic
interactions.
- These interactions stabilise the structure of the protein. The tertiary structure gives
rise to the overall three-dimensional shape of the protein.

Hydrogen bonding
- Hydrogen bond - A weak intermolecular force that exists when electronegativity creates a
polar covalent bond.
- Hydrogen bonding between polar R-groups in the tertiary structure of a protein
plays a crucial role in stabilising its three-dimensional shape by holding distant
regions of the polypeptide chain together. This stabilising effect is critical for
maintaining the protein’s functional integrity and any slight deviations from the
correct structure can impair the activity of the protein significantly.
- A hydrogen atom forms a link between two electronegative atoms, such as O or N.
In example the hydrogen bond is between O and OH.
Ionic bond
- Ionic bonding is a type of chemical bond that forms between oppositely charged ions.
- In proteins, the R-group can undergo binding or dissociation of hydrogen ions,
resulting in a positively or negatively charged state, respectively.
- These charged R-groups can then interact with oppositely charged atoms in other
molecules, forming ionic bonds. These ionic bonds can further contribute to the
overall stability and function of the protein.
 - Ionic bonds between positively charged and negatively charged R-groups. Amine
+¿ ¿
+ ¿→ N H 3 ¿

groups become positively charged ( N H −¿+

2
H ¿
. Carboxyl groups become
negatively charged by donating a proton ¿. Because of the involvement of protons
(hydrogen ions), ionic bonds in proteins are sensitive to pH changes.
- Students should understand that amine and carboxyl groups in R-
groups can become positively or negatively charged by binding or
dissociation of hydrogen ions and that they can then participate in ionic
bonding.
Disulfide covalent bonds/Disulfide bridge
- Disulfide covalent bonds form between pairs of cysteine amino acid residues,
which contain sulphur atoms(Single covalent bond between sulphurs). These bonds
are critical for stabilising the tertiary and quaternary structures of proteins by forming
covalent bonds that help to maintain the protein’s overall three-dimensional shape,
contributing to its stability and function.

-
Hydrophobic interactions
- Hydrophobic interactions occur between non-polar amino acids. This occurs as water
is a polar molecule and forms hydrogen bonds with polar amino acids. As the non-
polar amino acids are unable to interact with water, they tend to clump together
into hydrophobic clusters in the interior of the protein, to minimise contact with
the surrounding water molecules. These hydrophobic interactions stabilise the
protein’s tertiary structure and quaternary structures.

Strength of interactions within the tertiary structure (weakest to strongest)

● Hydrophobic interactions
● Hydrogen bonds
● Ionic bonds
● Disulphide bridge/disulphide covalent bond
The tertiary structure develops as a polypeptide is synthesised by the ribosome, sometimes
with a chaperone protein. A wide range of three-dimensional shapes are produced, most of
which are globular. Within these tertiary structures, there are often parts with secondary
structures, alpha helixes and beta-pleated sheets. ‘
Effect of polar and non-polar amino acids on the tertiary structure of proteins

- Amino acids can be nonpolar and have no-charge → they can be classified
as hydrophobic
- Amino acids can be polar or be charged → they can be classified as
hydrophilic

Polar and non-polar amino acids affect the tertiary structure of proteins. Hydrophilic polar
amino acids orient to the outside towards the aqueous environment, whereas
hydrophobic non-polar amino acids are protected in the core, minimising unfavourable
interactions between hydrophobic side chains and water molecules.
- The resulting compact, folded conformation exposes hydrophilic surfaces to the
solvent and buries hydrophobic residues in the protein’s interior, thereby contributing
to protein stability and function.

Globular proteins have this arrangement of hydrophobic core and hydrophilic exterior. This
arrangement stabilises the tertiary structure of the protein because it maximises
hydrophobic interactions between amino acids in the centre and hydrogen bonding between
amino acids on the surface and the water around the protein.

- Globular proteins - Proteins that are compact and spherical in shape. They play
important roles as enzymes, transporters and regulators.
- Examples of globular proteins:
- Myoglobin - A protein found in muscle tissue that binds and stores
oxygen.
- Haemoglobin - The iron-containing protein present in red blood cells
that carries oxygen.
- Enzymes - biological catalysts used for speeding up metabolic
reactions
A protein responsible for transporting oxygen throughout the body, are both examples of
globular proteins with hydrophobic cores.

Integral proteins (attached to the membrane) have regions with hydrophobic amino acids,
helping them to embed in membranes. This is because they routinely come in contact with
non-polar substances. Integral proteins embedded in membranes have hydrophobic amino
acids where they contact the nonpolar hydrocarbon core of the membrane. In
transmembrane proteins (they span across the bilayer), this hydrophobic region is a belt,
with hydrophilic regions inside and outside that are in contact with aqueous solutions inside
and outside of the cell.

Channel proteins in membranes allow hydrophilic solutes or water to diffuse across the
hydrophobic core of the membrane. They have hydrophilic regions with a hydrophobic region
between, which holds them in a transmembrane position. They have a tunnel lined with
hydrophilic amino acids through the centre of the protein. The width and charge distribution
of this channel allows specific hydrophilic ions or molecules to pass through.

Transmembrane proteins- Transmembrane proteins are firmly inserted into the

phospholipid bilayer. Spanning the entire width of the membrane, they may protrude from
both sides of the cell. The columnar transmembrane proteins make up about half of the cell
membrane by mass and are responsible for the specialised membrane functions.

The quaternary structure of non-conjugated and conjugated proteins

Quaternary structure - Structure of a protein refers to the arrangement and interaction of

two or more polypeptide chains to form a functional protein.

In proteins that consist of more than a single polypeptide, the three-dimensional

arrangement of subunits is the quaternary structure. The quaternary structure of a protein
refers to the arrangement and interaction of two or more individual polypeptide chains.
 - An example of a protein that has quaternary structure is haemoglobin, which
consists of four individual polypeptide chains: two of which are designated ‘ɑ-
chains’ and two which are designated ‘β-chains’

Conjugated protein - Proteins that contain a non-protein component such as a metal ion or
a carbohydrate.
- Conjugated proteins have one or more non-polypeptide subunits in addition to their
polypeptides.
- Haemoglobin consists of four polypeptide chains, each associated with a haem
group. The haem group of haemoglobin binds oxygen. (See diagram above)
- Many enzymes have a non-polypeptide component that contributes to the catalytic
activity of their active site

-
- The four subunits of haemoglobin are held together by non-covalent bonds, and the
interactions between the subunits allow haemoglobin to undergo conformational
changes necessary for its oxygen-carrying function. The quaternary structure of
haemoglobin is essential for its biological function and highlights the complexity and
 importance of protein structure in biological systems.

- While some proteins may be non-conjugated, others may be conjugated. Conjugated

proteins have non-protein components such as metal ions or carbohydrates in
addition to having polypeptide subunits. These non-protein components have the
ability to increase a protein’s diversity and functionality. For example, non-
protein components play a crucial role in many enzymes, helping them perform their
catalytic functions.
- Technology allows imaging of structures that would be impossible to observe with the
unaided senses. Cryogenic electron microscopy has allowed imaging of single-
protein molecules and their interactions with other molecules.

Non-conjugated proteins have only polypeptide subunits. It requires the same types of
interaction as a tertiary structure to form a quaternary structure.
- Insulin has two polypeptides linked by disulfide bonds.
- Collagen consists of three polypeptides wound together to form a rope-like structure
with high tensile strength.

Relationship of form and function in globular and fibrous proteins

- The structure of a protein determines its function as it allows the protein to interact
with other molecules and its environment. Differences in shape, solubility and
function are due to differences in the amino acid composition and the way the
polypeptide chains are folded and arranged.
- After a polypeptide chain is synthesised, it undergoes a process called protein
folding in which it adopts a specific three-dimensional shape that is critical for its
proper function. The folding process is influenced by various chemical and physical
forces, such as hydrogen bonding, ionic bonding and hydrophobic interactions, and is
determined by the sequence of amino acids in the protein as well as the cellular
 environment in which it is synthesised. Once proteins take their final form, they can
be classified as either globular or fibrous.

-
- Globular proteins are complex proteins that are usually spherical in shape with
irregular folds. They are soluble in water and play important roles as enzymes ,
transporters and regulators. Insulin is an example of a globular protein that consists
of two polypeptide chains: the ɑ-chain and β-chain. They are arranged in a specific
three-dimensional shape that is held together by hydrogen bonds, hydrophobic
interactions and disulfide bonds. Mainly disulphide bonds

- Insulin is globular with a hydrophilic exterior and a hydrophobic interior. The

hydrophilic exterior allows insulin to interact with water and other hydrophilic
molecules in the blood. This is important because insulin needs to travel
through the bloodstream to reach its target tissues, and bind to its
receptors. The hydrophobic interior of the insulin protein helps to stabilise the
shape of the protein, allowing it to maintain its globular shape, which is
essential for the insulin to bind to its receptor.
- Insulin - A hormone that regulates glucose levels in the bloodstream
by facilitating glucose uptake and storage in cells. It is produced by
the pancreas and released into the bloodstream in response to high
blood sugar levels. Insulin binds to specific receptors on cells, allowing
glucose to enter the cells and be used for energy or stored for later
use.
Globular proteins have a rounded/spherical shape formed by the irregular folding of
polypeptides and are soluble. The shape is very intricate and is stabilised by the bonds
between the R-groups of the amino acids that have been brought together by folding. Some
globular proteins are conjugated proteins that contain a prosthetic group (e.g. haemoglobin)
- Insulin molecule has the conformation needed to bind to a specific site on the insulin
receptor. This allows a specific and unambiguous signal to be sent to body cells
when body sugar concentration is too high.
- Insulin consists of two polypeptide chains: the ɑ-chain and β-chain

Fibrous proteins consist of elongated polypeptides that lack the folding of typical tertiary
structures and are insoluble. They also do not develop secondary structures like alpha
helices. Their quaternary structure is developed by linking together polypeptide chains into
narrow fibres or filaments, with hydrogen bonds between the chains. It tends to be
insoluble due to the large amount of hydrophobic R groups.
- Collagen is a fibrous protein with a quaternary structure of three polypeptides wound
together into a triple helix. It has a primary structure of a repeating sequence of
three amino acids: P-G-X. The winding together of the three helices would be
impossible if there were an alpha helix. The P (proline) has a special property that
prevents the formation of an alpha helix. The rope-like structure of collagen
gives its very high tensile strength. The R-group of amino acid X faces outwards
and is variable, allowing many variations of collagen to be produced.
- The fibres are very strong and flexible, resisting forces without breaking. This
provides structural support to tissues, helping them to maintain their shape
and integrity.

-
Collagen
- It's found in skin, hair, nails, tendons, cartilage, and bones. Collagen works
with other substances, such as hyaluronic acid and elastin, to maintain skin
elasticity, volume, and moisture.
Importance of polar and nonpolar proteins in amino acids
Functions of proteins
4 structures of protiens