ASSIGNMENT BIOCHEMISTRY

Group10

Name MEMBER:

1.Leng Setha

2.Sok Nita 3.Song Kimheang

4.Sorn Munineath 5.Tang Sarin

6.Thav Yuoeng 7.Sao Sina

8.Sroeun Ratana 9.Chuo Peaktra

1. Definition
Keratin , fibrous structural protein of hair, nails, horn, hoofs, wool,

feathers, and of the epithelial cells in the outermost layers of the

skin.
2. Classification

Keratin proteins can be subdivided into alpha-keratins and beta-keratins, on the basis of

their secondary structure (the geometry of their polypeptide chains, which is influenced

by hydrogen bonding). Alpha-keratins, which are found in the hair, the skin, and the wool

of mammals, are primarily fibrous and helical in structure. By contrast, beta-keratins,

which occur in birds and reptiles, consist of parallel sheets of polypeptide chains .
3. Alpha Keratin

Alpha-keratin, or α-keratin, is a type of keratin found in vertebrates. This protein is the

primary component in hairs, horns, mammalian claws, nails and the epidermis layer of

the skin. 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 coil. Due to its
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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.

3.1 Structure
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 termini bonding with the termini 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 either is high

in cysteine or glycine, tyrosine, and phenylalanine residues. The different types,

alignments, and matrices of these IFs account for the large variation in α-keratin

structures found in mammals.

3.2 Synthesis

α-keratin synthesis begins near focal adhesions on the cell membrane. There, the keratin

filament precursors go through a process known as nucleation, where the keratin

precursors of dimers and filaments elongate, fuse, and bundle together. As this synthesis

is occurring, the keratin filament precursors are transported by actin fibers in the cell

towards the nucleus. There, the alpha-keratin intermediate filaments will collect and form

networks of structure dictated by the use of the keratin cell as the nucleus simultaneously

degrades. However, if necessary, instead of continuing to grow, the keratin complex will

disassemble into non-filamentous keratin precursors that can diffuse throughout the

cell cytoplasm. These keratin filaments will be able to be used in future keratin synthesis.

When the cell has been filled with the correct keratin and structured correctly, it

undergoes keratin stabilization and dies. Alpha-keratin cells are the main components of

hair, the outer layer of nails and horns, and the epidermis layer of the skin.

3.3Properties

Keratin is completely insoluble in hot or cold water and is not attacked by proteolytic

enzymes

3.4Type

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 or hair.

4. Function

Hard and soft

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.

Keratin serves important structural and protective functions, particularly in the epithelium.

Some keratins have also been found to regulate key cellular activities, such as cell growth
and protein synthesis. Keratin use as an ingredient cosmetics.

5. Conclusion and Recommendation

Keratin is the hard protein that makes up your hair, nails, and the

outer layer of your skin. Increasing your keratin may help give

more flexibility, strength, and shine. Deficiency of keratin can result

in hair loss, sagging skin and nail breakage.

You can increase your keratin naturally by eating a diet rich in keratin and other nutrients,

and try using products that contain or increase keratin.

6.Reference

https://www.wikihow.com/Increase-Keratin

https://en.wikipedia.org/wiki/Alpha-keratin

https://www.britannica.com/science/phase-state-of-matter

https://www.sciencedirect.com/