Structure of
Keratin
Introduction
Fibrous (structural) proteins.Individual molecules
combine to form insoluble structures
Keratins are the molecular basis for hair, nails, wool,
feathers, beaks, claws and horns.
It is also found in the cytoskeleton of cells. Keratin
clusters are found on chromosomes 12 and 17. α-keratin
is a fibrous structural protein, meaning it is made up of
amino acids that form a repeating secondary structure.
The secondary structure of α-keratin is very similar to
that of a traditional protein α-helix and forms a coiled
structure
Due to its tightly wound structure, it can function as one
of the strongest biological materials and has various
functions in mammals, from predatory claws to hair for
warmth.
α-keratin is synthesized through protein biosynthesis,
utilizing transcription and translation, but as the cell
α-keratin is a polypeptide chain, typically high in alanine,
leucine, arginine, and cysteine, that forms a right-handed
α-helix.
Two of these polypeptide chains twist together to form a
left-handed helical structure known as a coiled coil.
These coiled coil dimers, approximately 45 nm long, are
bonded together with disulfide bonds, utilizing the many
cysteine amino acids found in α-keratins.
The dimers then align, their terminal bonding with the
terminal of other dimers, and two of these new chains
bond length-wise, all through disulfide bonds, to form a
protofilament.
Two protofilaments aggregate to form a protofibril, and
four protofibrils polymerize to form the intermediate
filament (IF).
The IF is the basic subunit of α-keratins. These IFs are
able to condense into a super-coil formation of about 7
nm in diameter, and can be type I, acidic, or type II, basic.
The IFs are finally embedded in a keratin matrix that
Characterization
Alpha-keratins proteins can be one of two types: type I or type II.
There are 54 keratin genes in humans, 28 of which code for type
I, and 26 for type II.
Type I proteins are acidic, meaning they contain more acidic
amino acids, such as aspartic acid, while type II proteins are
basic, meaning they contain more basic amino acids, such as
lysine.
This differentiation is especially important in alpha-keratins
because in the synthesis of its sub-unit dimer, the coiled coil, one
protein coil must be type I, while the other must be type II.
Even within type I and II, there are acidic and basic keratins that
are particularly complementary within each organism.
For example, in human skin, K5, a type II alpha keratin, pairs
primarily with K14, a type I alpha-keratin, to form the alpha-
keratin complex of the epidermis layer of cells in the skin.
Properties
The property of most biological importance of alpha-
keratin is its structural stability.
When exposed to mechanical stress, α-keratin structures
can retain their shape and therefore can protect what
they surround.
Under high tension, alpha-keratin can even change into
beta-keratin, a stronger keratin formation that has a
secondary structure of beta-pleated sheets.
Alpha-keratin tissues also show signs of viscoelasticity,
allowing them to both be able to stretch and absorb
impact to a degree, though they are not impervious to
fracture.
Alpha-keratin strength is also affected by water content
in the intermediate filament matrix; higher water
content decreases the strength and stiffness of the
keratin cell due to their effect on the various hydrogen
Hard alpha-keratins, such as those found in nails, have a
higher cysteine content in their primary structure.
This causes an increase in disulfide bonds that are able to
stabilize the keratin structure, allowing it to resist a
higher level of force before fracture.
On the other hand, soft alpha-keratins, such as ones
found in the skin, contain a comparatively smaller amount
of disulfide bonds, making their structure more flexible.
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