Post Translational Modification
Post Translational Modification - Related Videos
10:07
Identification of Post-translational Modifications of Plant Protein Complexes
0 Views •
Cited by 8 •
2014
We describe here a protocol for the purification and characterization of plant protein complexes. We demonstrate that by immunoprecipitating a single protein within a complex, so we can identify its post-translational modifications and its interacting partners.
07:13
Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA
0 Views •
Cited by 8 •
2011
Nucleosome ELISA (NU-ELISA) is a sensitive and quantitative method to detect global patterns of post-translational modifications in preparations of native, intact nucleosomes. These modifications include methylations, acetylations, and phosphorylations at specific histone amino acid residues, and hence NU-ELISA provides a global proteomic assay of the overall chromatin modification states of specific cell types.
05:56
Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
0 Views •
Cited by 1 •
2022
The present protocol uses a biomolecular simulation package and describes the molecular dynamics (MD) approach for modeling the wild-type caspase and its mutant forms. The MD method allows for assessing the dynamic evolution of the caspase structure and the potential effect of mutations or post-translational modifications.
09:22
Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
0 Views •
Cited by 22 •
2013
The preparation of high quality yeast cell extracts is a necessary first step in the analysis of individual proteins or entire proteomes. Here we describe a fast, efficient, and reliable homogenization protocol for budding yeast cells that has been optimized to preserve protein functions, interactions, and post-translational modifications.
09:29
Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
0 Views •
Cited by 5 •
2017
In this method, we present biochemical procedures for rapid and efficient isolation of intermediate filament (IF) proteins from multiple mouse tissues. Isolated IFs can be used to study changes in post-translational modifications by mass spectrometry and other biochemical assays.
FAQs
Adding a phosphate, acetyl, methyl group, or ubiquitin can change a protein’s charge, three-dimensional conformation, or binding interactions. These chemical changes may alter whether the protein interacts with other molecules, where it is localized within the cell, how active it is, or how long it persists. Consequently, one gene sequence can support multiple functionally distinct protein states.
Enzymes control PTM patterns by attaching or removing specific functional groups and molecular units from proteins. Their activity connects protein chemistry to cellular signals and changing conditions, allowing protein properties to shift in response to the cell’s state. This enzymatic control can influence activity, localization, molecular recognition, and degradation pathways rather than producing a fixed protein outcome.
A chemical group added to a protein can alter its charge or promote a different conformation, meaning the protein adopts a changed three-dimensional arrangement. Those effects can modify binding interactions and accessibility of functional regions. In chemistry and biochemistry, tracking these changes helps explain how a covalent modification is translated into altered protein activity or cellular behavior.
Mass spectrometry provides an analytical route for identifying where modifications occur on proteins. Detecting modification sites connects a chemical change with a particular protein region, helping researchers relate PTMs to altered structure, activity, localization, or lifetime. The resulting site information also supports studies of signaling networks, disease mechanisms, biomarker discovery, and therapeutic development.
PTM research is closely connected to signaling networks, gene regulation, metabolism, and disease mechanisms. Modifications can change protein interactions, activity, localization, or degradation, so they help explain how cells coordinate these processes. Studying the chemical changes provides a way to connect molecular events after protein synthesis with broader cellular regulation and abnormal states associated with disease.
Because PTMs can reflect changes in protein activity, localization, interactions, or lifetime, their sites and patterns may provide measurable indicators of cellular state. Analytical identification of those changes supports biomarker discovery and can reveal chemically regulated processes relevant to disease. The same information contributes to therapeutic development by highlighting protein behaviors and regulatory pathways that may require intervention.