Protein: Globular and Fibrous Protein

Protein
Globular And Fibrous Protein

What is Globular Protein ?
• Globular proteins or spheroproteins are spherical "globe-like" proteins and
are one of the common protein types (the others
being fibrous, disordered and membrane proteins). Globular proteins are
somewhat water-soluble (forming colloids in water), unlike the fibrous or
membrane proteins.
• Examples of globular proteins include haemoglobin, insulin and

many enzymes in the body.
Structure of The Globular proteins
• Globular proteins have a 3D molecular structure that has a shape that is anywhere from a sphere to a
cigar. Usually the structure of a globular protein is divided into three or four levels. The primary
structure is simply the sequence of amino acids forming the peptide chain. The peptide chain can be
folded in an ordered and repetitive fashion, and the structures with ordered and repetitive
conformations are called secondary structures. Helices, β-sheets and turns are three important types of
secondary structures. Turns are classified as a secondary structure even though their structures are
ordered but not repetitive. The tertiary structure is the overall 3D structure of a globular protein and is
produced by folding the helices and sheets upon themselves with turns and loops forming the folds.
• The spherical structure is induced by the protein's tertiary structure. The molecule's non

polar (hydrophobic) amino acids are bounded towards the molecule's interior whereas polar
(hydrophilic) amino acids are bound outwards, allowing dipole-dipole interactions with the solvent,
which explains the molecule's solubility.
• Globular proteins are only marginally stable because the free energy released when the protein folded
into its native conformation is relatively small. This is because protein folding requires entropic cost.
As a primary sequence of a polypeptide chain can form numerous conformations, native globular
structure restricts its conformation to a few only. It results in a decrease in randomness, although non-
covalent interactions such as hydrophobic interactions stabilize the structure.
Hemoglobin
• Hemoglobin is the iron- containing oxygen-transport metalloprotein in the

red blood cells of almost all vertebrates. It is a protein having a globular
structure. Based on its structural properties, hemoglobin can be divided
into two parts; a protein part and a heme group.
• The structure of the protein part can be studied at four levels; primary
structure, secondary structure, tertiary structure, and quaternary structure.
3-Dimensional Structure of hemoglobin a Globular Protein
Functions of the Hemoglobin
• Impacts red color to the blood.
• Helps to carry out the oxygen and other gases assisting the
respiratory system.
• It buffers the blood pH and maintains it to the tolerance limits.
• Source of physiological active catabolites.
• Genetic resistance to malaria. etc

Structure of Hemoglobin
Primary Structure
primary structure of proteins deals with the number and sequence of amino acids
in a polypeptide chain. One molecule of hemoglobin is made up of four
polypeptide chains; two alpha chains and two beta chains.The number of amino
acids is different in both types of polypeptide chains.
Each alpha chain contains 141 amino acids.

Each beta chain contains 146 amino acids.
Thus, a total of 574 amino acids are present in one molecule of amino acid. The
sequence of amino acids in alpha chains is different than that of the beta chain.
Any disturbance in the normal sequence of amino acids impairs the normal
functioning of hemoglobin.
Secondary Structure
• Secondary structure deals with the stable structures formed by
polypeptide chains. In the structure of hemoglobin, each alpha
and beta chain has an alpha-helical structure. These alpha
helices are held together via hydrogen bonding. They are
terminated by the presence of either proline amino acid or by
beta bends and loops connecting the different helices.
Tertiary Structure
• The tertiary structure involves the folding of polypeptide

chains. Alpha and beta chains undergo folding to attain a
globular shape. This folding of polypeptide chains occurs in
such a way that the hydrophilic amino acids are exposed on
the surface of the molecule while the hydrophobic amino acids
are buried inside the globular structure. The hemoglobin
molecule thus formed is composed of four subunits and thus,
is called a tetramer.
Quaternary Structure
The quaternary structure involves the arrangement of multiple polypeptide chains within the same
molecule. One hemoglobin molecule is made up of four subunits and thus, is called a tetramer.
Hemoglobin tetramer is considered to be composed of two identical dimers.
Each dimer is formed by one alpha chain and one beta chain. The two chains within each dimer are held
together via hydrophobic interactions.
On the other hand, the two dimers are linked to one another via weak polar interactions. These weak
attractive forces allow the dimers to move relative to one another. As a result, the two dimers occupy
different positions in oxygenated and deoxygenated forms of hemoglobin.
Based on the oxygenation status, hemoglobin can have the following two forms;
• T form: The ‘T’ or taut (tense) is the deoxy form of hemoglobin. During this state, the two dimers are
held together via ionic and hydrogen bonds. These bonds limit the movement of the polypeptide chains,
thus called the taut or tense (T) form.
• R form: The oxygenated form of hemoglobin is called the ‘R’ (relaxed) form. When oxygen binds to a
molecule of hemoglobin, it causes the breaking of weaker polar forces among the two dimers. This
allows the polypeptide chains to undergo some movement, thus called the relaxed (R) form.
Structure of Heme
Heme is the most important structural component of hemoglobin. It is complex formed by

protoporphyrin IX and a ferrous ion (Fe+2). It is a planar cyclic compound having one ferrous ion at
its center. This ferrous ion can form two additional bonds, one with the oxygen molecule and one
with the amino acid. These bonds are formed on two sides of the planar protoporphyrin ring.
One heme group is coupled with each polypeptide chain in hemoglobin. It is attached to the alpha
or beta chain via a bond between ferrous ion and the side chain of histidine. Thus, four heme
groups are present in one molecule of hemoglobin. Therefore, one hemoglobin molecule carries
four molecules of oxygen.
What is Fibrous Protein ?
• Scleroproteins or fibrous proteins is one of the three
main classification of protein structure (alongside globular and membran
proteins). These kind of protein can be distinguished from globular protein
by its low solubility in water. The roles of such proteins include protection
and structural role by forming connective tissue, tendons, bone matrices,
and muscle fiber.
Structure of Fibrous Protein
Fibrous proteins are made up of polypeptide chains that are elongated and fibrous in nature or
have a sheet like structure. They are generally water-insoluble and are found as an aggregate due
to hydrophobic R-groups that stick out of the molecule.. They are often structural proteins that
provide strength and protection to cells and tissue. The amino acid sequences they are made from
often have limited residues with repeats. These can form unusual secondary structures,
e.g. collagen triple helix. The structures often contain 'cross-links' between chains, for example
cys-cys disulphide bonds between keratin chains. Fibrous proteins often play a structural role in
nature. For example, α-keratin is composed of α-helical segments of polypeptides and is the
predominant constituent of claws, fingernails, hair, and horn in mammals. The structure of the α-
keratin is dominated by α-helical segments of polypeptide. The structure of the central rod
domain of a typical α-keratin is shown below. Pairs of right-handed helices wrap around each
other to form a left-twisted coiled coil.
Collagen
• Collagen is a rigid, inextensible fibrous protein that is
composed pf three intertwined polypeptide chains and is
a principal constituents of connective tissue in animals,
including tendons, cartilages, bones, teeth, skin and
blood vessels.
Tropocollagen triple helix
Functions of the Collagen
• Imparts strength, support, shape and elasticity to the tissue.
• Provides flexibility, support and movement to cartilage.
• Encases and protects delicate organs like kidney and spleen.
• Fills the sclera of the eye in crystalline form.
• Teeth(dentine) are made by adding mineral crystals to collagen.
• Contributes to proper alignment of cells for cell proliferation and

differentiation.
• When exposed to damaged blood vessels, it initiates thrombus formation.

Structure of Collagen
• Collagen is a fibrous protein consisting of three polypeptide chains
wound around each other. Each of the three chains is a coil itself.
Hydrogen bonds form between these coils, which are around 1000
amino acids in length, which gives the structure strength. This is
important given collagen’s role, as structural protein. This strength
is increased by the fact that collagen molecules form further chains
with other collagen molecules and form Covalent Cross Links with
each other, which are staggered along the molecules to further
increase stability. Collagen molecules wrapped around each other
form Collagen Fibrils which themselves form Collagen Fibres.
triple-helical structure of collagen
• The triple-helical structure of collagen arises from an unusual abundance
of three amino acids: glycine, proline, and hydroxyproline. These amino
acids make up the characteristic repeating motif Gly-Pro-X, where X can
be any amino acid. Each amino acid has a precise function. The side chain
of glycine, an H atom, is the only one that can fit into the crowded center
of a three-stranded helix. Hydrogen bonds linking the peptide bond NH of
a glycine residue with a peptide carbonyl (C═O) group in an
adjacent polypeptide help hold the three chains together. The fixed angle
of the C – N peptidyl-proline or peptidyl-hydroxyproline bond enables
each polypeptide chain to fold into a helix with a geometry such that three
polypeptide chains can twist together to form a three-stranded helix.
Interestingly, although the rigid peptidyl- proline linkages disrupt the
packing of amino acids in an α helix, they stabilize the rigid three-stranded
collagen helix.
Fibrous and Globular Proteins Structural Comparision

Protein: Globular and Fibrous Protein

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Protein

Globular And Fibrous Protein

• Examples of globular proteins include haemoglobin, insulin and

• The spherical structure is induced by the protein's tertiary structure. The molecule's non

• Hemoglobin is the iron- containing oxygen-transport metalloprotein in the

• It buffers the blood pH and maintains it to the tolerance limits.

• Source of physiological active catabolites.

• Genetic resistance to malaria. etc

Each alpha chain contains 141 amino acids.

• The tertiary structure involves the folding of polypeptide

Heme is the most important structural component of hemoglobin. It is complex formed by

• Provides flexibility, support and movement to cartilage.

• Encases and protects delicate organs like kidney and spleen.

• Fills the sclera of the eye in crystalline form.

• Teeth(dentine) are made by adding mineral crystals to collagen.

• Contributes to proper alignment of cells for cell proliferation and

• When exposed to damaged blood vessels, it initiates thrombus formation.

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