Services for Protein Liquid-Liquid Phase Separation
Intrinsically disordered proteins (IDPs), also known as functional proteins lacking stable secondary and/or tertiary structures, exist as highly dynamic and heterogeneous conformational ensembles, which are widespread in the protein field and have triggered a paradigm shift in biochemistry. With the advent of the post-genomic era, the field of structural disorders has benefited from spectacular developments in structural biology. IDPs have the ability to perform liquid-liquid phase separation (LLPS), which can drive the formation of biomolecular condensates assembled from protein and RNA molecules. Despite intensive studies on LLPS of biomolecules in recent years, our understanding of the prevalence and distribution of phase-separated proteins still lags behind. Furthermore, several proteins have now been shown to undergo phase separation in the test tube, but the in vitro or intracellular molecular structures associated with these phase-separated states are still hotly debated.
Fig. 1. Functions of intrinsically disordered proteins (IDPs). (Brocca S, et al., 2020)
Customized Services
Many of the proteins that undergo phase separation are present in several different membraneless organelles. Since the function of these IDPs derives from their unique structure, and since protein dynamics has been considered a major determinant of protein activity, our team of experts is focused on developing a new paradigm of "kinetic-functional relationships" from an experimental and computational perspective. CD BioSciences offers specialized structure and dynamics services of phase-separated protein to analyze the relationship between structure and function of phase-separated proteins.
Our proteomics and genetics approaches can determine the protein composition of a wide range of membraneless organelles. Leveraging prior insights from polymer chemistry has greatly improved our understanding of phase-separated proteins and inspired new approaches to further explore their underlying biochemistry and structural biology. As your ideal partner, CD BioSciences offers comprehensive liquid-liquid phase separation services of proteins to analyze their dynamic properties in phase-separated protein systems and their relevance to their formation, function, and physiopathology.
Computational Screening Service for Phase-Separated Proteins
Proteins that can phase separate in cells have typical sequence features such as intrinsically disordered regions (IDRs) and multiple modular structural domains. We provide sequence-based analysis tools to screen these proteins. In addition, we develop a series of useful bioinformatics tools to predict phase separated proteins.
Post-Translational Modifications in Liquid-Liquid Phase Separation
Protein post-translational modification (PTM) is a rapidly regulated and reversible process that controls life processes and is a subsequent step in protein translation. We help our clients analyze the regulation of LLPS by various PTMs, including phosphorylation, acetylation, poly (ADP-ribosyl)-ation (PAR), ubiquitination and methylation.
Why Choose Us
- Provide structural and functional information on phase-separated proteins.
- Purification and high-resolution structural studies of membraneless organelles.
- Inspire the design of novel biomaterials.
- Open up new avenues for targeting abnormal protein phase transitions in human diseases.
CD BioSciences is committed to solving the structural and functional enigma of biomolecular condensates from the perspective of phase-separated proteins. We focus on intrinsic IDPs because the structural plasticity of such proteins determines their ability to undergo LLPS and the important role they play in the formation and function of biomolecular condensates. If you have any special requirements for our services, please feel free to contact us. We are looking forward to working together with your attractive projects.
Reference
- Brocca S, et al. (2020) Liquid-Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus-Host Interactions. Int J Mol Sci. 21(23):9045.
For research use only, not intended for any clinical use.
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