Proper folding is required for most proteins to adopt a defined conformation in order to display their biological function. They denature and unfold whenever they lose their unique native conformation. Conformational changes and misfolding of proteins have been shown to be the underlying causes of disease. With years of experience, we provide customized protein conformational isomerism detection and analysis service to precisely meet customer requirements.

Introduction of Protein Conformational Isomerism

Denatured proteins are usually mixtures containing multiple conformers. The transition between the conformations of native and denatured proteins, known as protein folding, is one of the most difficult and demanding challenges in protein engineering. Alterations in protein structure, including mutations, modifications, conformational changes, and misfolding, play an important role in the development of disease. Within the cell, the accumulation of misfolded proteins is sensed and regulated by a cascade of folded protein reactions, and a small fraction of correctly folded proteins may denature and unfold under conditions similar to the extracellular environment. The biological function of denatured proteins requires careful regulation of protein conformational changes. Researchers are working to develop methods that can capture, separate, and characterize related protein isoforms that occur along protein conformational changes.

Fig 1. Reversible conversion between the native (N) and denatured X-isomers using the technique of disulfide scrambling. (Chang J Y, 2009)

Services

The conformers of denatured unfolded proteins are abundant in number and shape, and are abundant biomolecular resources. However, due to their instability and dynamic interconversion, it is inherently difficult to separate and characterize pure or structurally defined conformers. As a leading service provider of protein engineering, Creative BioMart has successfully established a protein conformational isomerism detection and analysis platform to capture selected conformers of denatured proteins that are easy to separate, characterize and further apply.

The technique of disulfide scrambling permits reversible conversion between the native and diverse denatured isomers. We generate and isolate multiple non-native protein isoforms (X-isoforms) by disulfide scramble technology. In addition, based on the comprehensive structural analysis of the denatured state of proteins based on this technology platform, the structures of more than 25,000 native proteins have been determined.

Applications of Protein Conformational Isomerism Detection

• Comprehensive structural characterization of denatured proteins
• Elucidation of protein folding pathways
• Production of unlimited structurally defined non-native protein isoforms for biomedical applications

Creative BioMart is committed to providing global customers with high-quality protein conformational isomerism detection and analysis services, and providing solutions for the capture, separation and characterization of related protein isomers that appear along the process of protein conformational changes. We will work with you to develop the most appropriate strategy and provide the most meaningful data for your research for accelerating the research of life sciences. If you are interested in our services, please do not hesitate to contact us for more information.

Reference

1. Chang J Y. (2009) Conformational isomers of denatured and unfolded proteins: methods of production and applications[J]. The protein journal. 28(1): 44-56.

• Detection of Errors in Protein Models
• Folding and Molecular Simulation Service
• Molecular Docking Service
• Protein Crystallization Service
• Protein Model Ranking and Analysis Service