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4 Proteins

Proteins are large organic compounds composed of amino acids that perform various functions in living organisms, including support and enzyme catalysis. Amino acids, which contain both amino and carboxyl groups, can form polypeptides through condensation reactions, leading to the diverse structures and functions of proteins. Proteins can be classified into globular and fibrous types, with distinct characteristics and roles, such as hemoglobin for oxygen transport and collagen for structural support.

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4 views

4 Proteins

Proteins are large organic compounds composed of amino acids that perform various functions in living organisms, including support and enzyme catalysis. Amino acids, which contain both amino and carboxyl groups, can form polypeptides through condensation reactions, leading to the diverse structures and functions of proteins. Proteins can be classified into globular and fibrous types, with distinct characteristics and roles, such as hemoglobin for oxygen transport and collagen for structural support.

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amena562crash
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TOPIC: PROTEINS

Proteins are organic compounds of large molecular mass. They are not truly
soluble in water but form colloidal suspensions. In addition to carbon, hydrogen
and oxygen, they always contain nitrogen, usually Sulphur and sometimes
phosphorous. Whereas they are relatively few carbohydrates and fats, the
number of proteins is limitless. They are specific to each species. Glucose is
glucose in whatever organism it occurs but proteins vary from one species to
another. Indeed, it is the proteins rather than the fats and carbohydrates that
determines the characteristics of a species. Proteins are rarely stored in
organisms, except in the eggs or seeds where they are used to form new tissues.
Proteins perform many functions in living organisms. They are important
molecules that are involved in support, enzyme catalysis, transport, defence and
movement.
AMINO ACIDS
Amino acids are a group of over a hundred chemicals of which around 20
commonly occurs in proteins. They always contain a basic group, the amino group
(-NH2), and an acidic group, the carboxyl group (-COOH). Most amino acids have
one of each group and are therefore neutral, but few
have more amino groups than carboxyl ones (basic
amino acids) while others have more carboxyl than
amino groups (acidic amino groups). Histidine and
arginine are examples of basic amino acids; aspartic acid
and glutamic acid are examples of acidic amino acids.
All amino acids have a central carbon atom, an amine group and a carboxylic
acid group. Attached to the central carbon atom is a hydrogen atom and a group
that is specific to the type of amino acid. In the generalized amino acid this group
is known as R for residual.
Amino acids are soluble in water when they form ions. These ions are formed by
the loss of a hydrogen atom from the carboxyl group, making it negatively
charged. This hydrogen atom associates with the amino group making it positively
charged. This ion is therefore dipolar- having a positive and a negative pole. Such
ions are called zwitterions. Amino acids therefore have both acidic and basic
properties, i.e. they are amphoteric. Being amphoteric means they act as buffer
solutions. A buffer solution is one which resists the tendency to alter its pH even
when small amounts of acid or alkali are added to it. Such property is essential in
biological systems where any sudden change in pH could adversely affect the
performance of enzymes.

Amino Acid Abbreviation R group Comments


Glycine gly -H Smallest amino acid; many
found in collagen to allow for
close packing.
Methionine met -CH2-CH2-S-CH2 First amino acid of every
primary sequence when a
polypeptide is produced on a
ribosome.
Alanine ala -CH3 Non-polar R group
phe Non-polar R group, which has
Phenylalanin a ring structure formed of
e carbon atoms
Cysteine cys -CH2-SH Sulphur-containing R group;
forms covalent disulphide
bonds between parts of a
polypeptide or between poly
peptides.
TABLE SHOWING SOME AMINO ACIDS AND THEIR R-groups

Formation of Polypeptides
We have seen that monosaccharides may be linked to form disaccharides and
polysaccharides by the loss of water (condensation reaction). Similarly, a
formation of polypeptides follows the same pattern. A condensation reaction
occurs between the amino group of one amino acid and the carboxyl group of
another, to form a dipeptide. Further combinations of this type extend the length
of the chain to form a polypeptide.

When two amino acids are joined together a peptide bond is formed linking the C
of the carboxylic group of one amino acid with the N of the amine group of the
other. The addition of another amino acid forms a tripeptide etc. A polypeptide
usually contains hundreds of amino acids. Polypeptides may be linked by forces
such as disulphide bridges to give proteins compromising of thousands of amino
acids.
R Groups
R represents an R group that consists of one of various chemical structures,
ranging from a single hydrogen atom to a chain or ring of hydrocarbons for
example in phenylalanine and may also include Sulphur. The properties of
polypeptides and proteins are dependent on the R group that project from the
central chain. Some amino acids have polar groups so they attract water
molecules, but others are non-polar and do not. This means that polypeptides can
have a sequence of amino acids with non-polar R groups to form a hydrophobic
region that can pass through the central part of the phospholipid bilayer. Some R
groups ionize to form negatively or positively charged groups. These attract to
each other to form ionic bonds.
PROTEIN STRUCTURE
Polypeptides link together to form proteins which are arranged into four levels of
protein structure:
1. Primary structure- this structure refers to the sequence of amino acids in a
polypeptide chain. Eg:
2. Secondary structure- this structure refers to the twisting of the polypeptide
chain into a α-helix (e.g. keratin) or a β-pleated sheet (e.g. fibroin) due to
hydrogen bonds between hydrogen and oxygen. Eg:
3. Tertiary structure- this structure refers to the folding and bending of the
polypeptide on itself into a compact globule (for example all enzymes) due
to a combination of hydrogen bonds, ionic bonds, disulphide bonds and
hydrophobic interactions.
4. Quaternary structure- this structure refers to the combination of more
than one polypeptide, usually associated with non-protein groups
(prosthetic groups), for example in haemoglobin. This structure is due to a
combination of hydrogen bonds, ionic bonds and hydrophobic interactions
maintaining the polypeptides together. Eg: hemoglobin

Interactions between non-polar R groups of different amino acids form


hydrophobic interactions. This cause the protein to fold as hydrophobic side
groups are shielded from water. Where R groups contain sulphur disulphide
bonds can be formed between these groups, which contribute to the
maintenance of the tertiary protein structure.

TYPES OF PROTEINS
Proteins can either be globular proteins or fibrous proteins. They differ from each
other in the following ways:

GLOBULAR PROTEINS FIBROUS PROTEINS


It has polypeptide chains with irregular It has polypeptide chains with regular
sequences of amino acids. repetitive sequences of amino acids.
Its shape is a compact globule of It has long chains running parallel.
polypeptides.
It is chemically less stable and its It is chemically stable and relatively
activity is affected by factors such as unaffected by temperature,
its concentration, pH and concentration or pH.
temperature.
Each molecule of the same type of Each molecule of the same fibrous
globular protein has a specific protein may vary with slightly different
sequence. sequences of amino acids.
It is water soluble It is insoluble in water.
It is involved in various body systems Its role is mainly in helping to maintain
such as digestive system, endocrine structure and providing support.
system and the immune system.

An example of a globular protein is hemoglobin. It is also a conjugated protein


(i.e., having a prosthetic group) and consists of sequences of amino acids forming
four polypeptide chains that twist and fold into a compact shape and has heam as
the prosthetic group. Two chains alpha chains and the other two are beta chains
held together by hydrophobic interactions, hydrogen and ionic bonds.
Haemoglogin has a quaternary structure, with each haem group containing a
ferrous iron atom that is able to carry an oxygen molecule. Therefore, each
human hemoglobin molecule is capable of carrying four oxygen molecules,
making it an efficient respiratory pigment. This enables it to serve its vital function
in oxygen transport.
An example of a fibrous protein is collagen. It consists of a primary structure of a
repetitive tripeptide sequence that forms long chains and may run parallel to each
other. Its secondary structure has three unbranched polypeptide chains linked to
one another via cross bridges and forming a triple helix. These cross bridges
involve strong covalent bonds that help provide structural support the collagen
molecule, thereby making it resistant to stretching. Hence, collagen has an
important structural role in providing physical strength to connective tissues such
as tendons.
What are the 20 amino acids in the human body- names and abs.

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