Post translational modification can be defined as

The covalent or generally enzymatic modifications of proteins

durig of after the synthesis of the proteins.
Before understanding about it, first of all we
must have information about what is translation.
In molecular biology ,translation refrs to the formation of
proteins from mrna with the help of ribosomes present in the
cytoplasm of the cell in the case of prokaryotes while in
eukaryotes it is carried in the membrane of rer or in the
cytosol. the mrna then decoded from dna is migrated in to the
cytoplasm for the synthesis of protein that then fold, acquire
a tertiary conformation and perfom their perspective
functions.
Steps In post translational modifications:_
Initiation
Elongation
Termination
Types of post translational modifications are involved in
modifying the protein structure after they have been
translated according to information on the mRNA.
The post-translational modifications can be covalent or
enzymatic.
In the human body these ptms increase the diversity and
accuracy of proteins.
The types of post translational modifications are:
Trimming
Covalent attachment
Protein folding
Protein degradation
Trimming:-
Insulin is synthesized in the cells in the inactive form.for
proper functioning of insulin its past translational
modification occurs that involves the removal of the part of
the protein to convert it into a three dimensional and fully
active form.
Covalent attachment:
Refers to the addition or the transfer of the
polypeptide chain that acts as atn acceptor region. In this way
proteins are modified for the diversity of functions. It
includes:
Phosphorylation
Methylation
Glycosylation
Sulfation
Hydroxylation
Phosphorylation: is the addition of one or more phosphate
groups to the protein. Post translational phosphorylation is
one of the most common protein modifications that occur in
animal cells. The vast majorities of phosphorylation occur as a
mechanism to regulate the biological activity of a protein and
such are transient.
In animal cells, serine tyrosine and thereonine are the amino
acids that are subjected to this method.
Glycosylation:- is the addition of carbohydrate molecules to
the polypeptide chain and modifying it into glycoproteins.
Many of the proteins that are destined to be a part of the
plasma membrane or to b secreted from the cell, have
carbohydrate chains attached to the amide nitrogen of the
asparagine or the hydroxyl groups of sereine , threonine. N
glycosylation occurs in ER and O glycosylation in the Golgi
Complex.
Sulfation :- sulfate modification takes place by the addition
of the sulfate molecules and these modifications of proteins
occur at tyrosine residues. Tyrosine sulfation is accomplished
by the activity of TPSTs (tyrosylprotein sulfotransferases)
wich are membrane assosciated enzymes of trans-golgi
network. There are two tpsts :
Tpst 1
Tpst 2
The universal phosphate donor is 3 phosphoadenosyl 5 o
phosphosulphate (pspa).
METHYLATION:- the transfer of one carbon methyl group to
nitrogen or oxygen to amino acid side chains o the
hydrophobicity of the protein and can neutralize a negative
amino acid charge when bound to carbdoxylic acids. It is
mediated by methyltransferases and S- adenosyl methionine
is the primary methyl group donor.
HYDROXYLATION:- IS THE biological process of addition of
hydroxyl group to a protein amino acid. It is the type of ptm
that involves the conversion of a –CH group into –COH group
and hese hydroxylatedn amino acids are involved in the
regulation of some important factors called transcription
factors. Among 20, the two