To observe O-glycosylation in eukaryotic sequence.

Experiment #12   

Object:-

To observe O-glycosylation in eukaryotic sequence.

Theory:-

O- glycosylation occurs at Ser or Thr-residues, usually in sequence-stretches rich in hydroxy amino acids, but there has been no consensus sequence determined for this modification. In addition, O-glycosylation lacks a common core structure: mammalian proteins have been reported bearing O-linked N-acetylgalactosamine, fucose, glucose, and corresponding elongated structures, as well as N-acetylglucosamine. Chemical methods are used to liberate these oligosaccharides because no enzyme has been discovered that would cleave all the different O-linked carbohydrates. Glycosylation , a common PTM, plays a role in protein folding, transport and half-life, as well as being involved in cell-cell interactions and antigenicity. Glycosylation is an enzymatic process, with the exception of glycation, and involves the addition of sugars to the protein to build up glycan chains.

Procedure:-

1.NetOGly1.0 server was opened.

2. Fasta format was pasted in input box.

3.Result was noted.

DISCUSSION:-

In this experiment O-Glycosylation was observed.There is no any seqon.It has limited application.This tool is only for eukaryotic protein.O- glycosylation occurs at Ser or Thr-residues, usually in sequence-stretches rich in hydroxy amino acids, but there has been no consensus sequence determined for this modification. In addition, O-glycosylation lacks a common core structure.