AI Article Synopsis
- Posttranslational modifications (PTMs) can change a protein's structure, function, and location, making them key for cellular regulation and signaling.
- Advanced spectroscopic techniques help analyze how PTMs affect proteins and their interactions, but challenges arise due to the complexity and variability of modified proteins.
- Selective labeling with stable isotopes can simplify analyses, and the review highlights methods that combine chemical biology tools to study PTMs in proteins, leading to new biological insights.
Article Abstract
Posttranslational modifications can alter protein structures, functions and locations, and are important cellular regulatory and signalling mechanisms. Spectroscopic techniques such as nuclear magnetic resonance, infrared and Raman spectroscopy, as well as small-angle scattering, can provide insights into the structural and dynamic effects of protein posttranslational modifications and their impact on interactions with binding partners. However, heterogeneity of modified proteins from natural sources and spectral complexity often hinder analyses, especially for large proteins and macromolecular assemblies. Selective labelling of proteins with stable isotopes can greatly simplify spectra, as one can focus on labelled residues or segments of interest. Employing chemical biology tools for modifying and isotopically labelling proteins with atomic precision provides access to unique protein samples for structural biology and spectroscopy. Here, we review site-specific and segmental isotope labelling methods that are employed in combination with chemical and enzymatic tools to access posttranslationally modified proteins. We discuss illustrative examples in which these methods have been used to facilitate spectroscopic studies of posttranslationally modified proteins, providing new insights into biology.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8496066 | PMC |
| http://dx.doi.org/10.1039/d1cb00045d | DOI Listing |
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