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Post Translational Modifications

Most of the proteins that are translated from mRNA undergo chemical modifications before becoming functional in different body cells. The modifications collectively, are known as post-translational modifications. The protein post translational modifications play a crucial role in generating the heterogeneity in proteins and also help in utilizing identical proteins for different cellular functions in different cell types. How a particular protein sequence will act in most of the eukaryotic organisms is regulated by these post translational modifications.

Post translational modifications occurring at the peptide terminus of the amino acid chain play an important role in translocating them across biological membranes. These include secretory proteins in prokaryotes and eukaryotes and also proteins that are intended to be incorporated in various cellular and organelle membranes such as lysosomes, chloroplast, mitochondria and plasma membranes.

Expression of proteins is important in diseased conditions. Post translational modifications play an important part in modifying the end product of expression and contribute towards biological processes and diseased conditions. The amino terminal sequences are removed by proteolytic cleavage when the proteins cross the membranes. These amino terminal sequences target the proteins for transporting them to their actual point of action in the cell.

Protein post translational modifications may happen in several ways. Some of them are listed below:

  1. Glycosylation: Many proteins, particularly in eukaryotic cells, are modified by the addition of carbohydrates, a process called glycosylation. Glycosylation in proteins results in addition of a glycosyl group to either asparagine, hydroxylysine, serine, or threonine. Software for studying glycosylation by glycan structure prediction.

  1. Acetylation: the addition of an acetyl group, usually at the N-terminus of the protein.

  2. Alkylation: The addition of an alkyl group (e.g. methyl, ethyl).

  3. Methylation: The addition of a methyl group, usually at lysine or arginine residues. (This is a type of alkylation.)

  4. Biotinylation: Acylation of conserved lysine residues with a biotin appendage.

  5. Glutamylation: Covalent linkage of glutamic acid residues to tubulin and some other proteins.

  6. Glycylation: Covalent linkage of one to more than 40 glycine residues to the tubulin C-terminal tail of the amino acid sequence.

  1. Isoprenylation: The addition of an isoprenoid group (e.g. farnesol and geranylgeraniol).

  1. Lipoylation: The attachment of a lipoate functionality.

  1. Phosphopantetheinylation, The addition of a 4'-phosphopantetheinyl moiety from coenzyme A, as in fatty acid, polyketide, non-ribosomal peptide and leucine biosynthesis.

  1. Phosphorylation, the addition of a phosphate group, usually to serine, tyrosine, threonine or histidine.

  1. Sulfation: The addition of a sulfate group to a tyrosine.

  1. Selenation

  1. C-terminal amidation




An Innovative Glycan and Glycopeptide MSn Data Analysis Tool SimGlycan® predicts the structure of glycans and glycopeptides using mass spectrometry data.

SimGlycan® accepts the experimental MS/MS and Multi Stage/Sequential mass spectrometry (MSn, n>2) data, matches them with its own database of theoretical fragments and generates a list of probable candidate structures. Each structure is scored to reflect how closely it matches your experimental data. Apart from the structural information, other biological information for the probable molecular structures such as the glycan class (N-Linked, O-Linked heparin, lipopolysaccharide etc.), reaction, pathway and enzyme are also made available for easy reference in case of structural elucidation of glycans while in the case of glycopeptide qualitative analysis, information such as Protein ID, Protein Name, Source, Classification, Class, peptide sequence, peptide mass etc. are made available for identified glycopeptides.

Glycan & Glycopeptide MS/MS Data Analysis for Studying Glycosylation

Protein Glycosylation, which is a key post-translational modification, is the result of addition of a glycan to a peptide sequence. Glycopeptides are known to exhibit multiple biological functions. In order to identify distinct functional properties for defined structural features, detailed information on the respective glycan moieties is essential. In order to understand all these phenomena, glycosylation analysis is an area of growing interest. Glycans have also been found to participate in many biological processes including embryonic development, inter and intracellular activities, coordination of immune functions, pathogens homing on their host tissues, cell division processes and protein regulations and interactions.

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  • Robust Glycan and Glycopeptide Database
  • Support for MALDI MS/MS and LC-MS/MS Workflows
  • Data Input File Formats
  • Accurate Ranking Mechanism
  • Additional Filters For Precise Results
  • Comprehensive Result Analysis
  • LC-MS and LC- MS/MS Data Processing
  • High Throughput Analysis
  • TMT Quantitation
  • Multi Stage Mass Spectrometry (MSn) Data Analysis
  • Glycopeptide Qualitative Analysis
  • Project Management
  • Draw Glycans
  • Mass Spectra Interpretation

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