Analysis of Protein Stability of Sequence Evolution

With years of operational experience, Creative Biolabs is able to provide state-of-art services for any protein engineering-based projects. Our scientists specialized in protein stability analysis will work with you to develop a most appropriate strategy that will offer the most meaningful data for your research. Our mission is to help you meet current and future protein stability demand and clear the path to commercialization to help you stay at the forefront of protein engineering.

Introduction to Protein Stability

Protein stability has been considered as a hotspot in previous studies because of its specific contributions to disease therapy. Pilot studies have shown that a number of factors can affect the stability of a protein of interest, such as the folding state, hydrophobic cavities, water molecules, electrostatic interactions, as well as salt bridges. A more recent study has shown that mutations can also influence the stability of proteins by regulating the free energy of conformation states, including glycine, proline, and disulfide bridges. Meanwhile, recent researchers have demonstrated that the hydrophobic effect plays an important role in stabilizing the folded structures of various proteins. Moreover, many lines of evidence have revealed that proteins will become unstable at extreme pH because the charge repulsion caused by increased acidity or basicity can affect the folded form. As a result, a number of assays have been developed and widely used for analyzing the stability of different kinds of proteins. Among them, crystallography is a common method for determining the effect of long-range repulsion in different positive charges.

Fig.1 Analysis of Protein Stability of Sequence Evolution.

Services

In recent studies, protein engineering is focused on analyzing and improving the stability of various types of proteins. The analysis of protein stability is essential to reveal the mechanism of protein folding and design perfect protein molecules with many therapeutic applications. Furthermore, scientists have theorized that the condition of protein stability is also associated with the successful development of enzymes. In this condition, a wide collection of platforms have been developed by our company, which can offer a comprehensive assessment for protein stability, such as thermal shift assay, high-throughput assay as well as sequence evolution-based protein stability assay. For instance, the thermal denaturation of proteins has been monitored by using fluorescence dyes in our thermal shift assay. The data derived from real-time PCR (RT-PCR) has indicated that this assay can effectively analyze or improve the stability of different types of proteins. Furthermore, we have successfully developed a novel evolutionary strategy for screening amino acid sequences to analyze the thermodynamic and kinetic stability of the protein. Additionally, we also provide a number of protein stability optimization services to obtain the best protein for your projects.

Fig.2 Evolution of protein stability according to the model. (Kepp, 2014)

To meet the challenging requirements, Creative Biolabs has equipped a team of experienced scientists with facilities and processes designed specifically to provide the best strategy and protocols customized to protein stability services for protein engineering. We have successfully accomplished a number of projects and have delivered numerous results of protein stability analysis in a range of therapeutic areas. If you have any special needs in our protein stability analysis services or be interested in learning more about our company, please feel free to contact us for more details.

Reference

Kepp, K. P.; et al. A model of proteostatic energy cost and its use in the analysis of proteome trends and sequence evolution. PLoS One. 2014, 9(2): e90504.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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