Protein Characterization

These methods are comprised of different techniques such as polyacrylamide gel electrophoresis (PAGE) for molecular weight determination, western blot analysis for detection of specific molecules, surface plasmon resonance (SPR) analysis for studying the binding kinetics of molecular interactions, and CD-ORD spectroscopy for secondary structure determination.

This method serves as a preliminary analysis of the protein(s) of interest where the sample is passed through a gel and separated either in its native or linear conformations.

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This analysis detects specific epitopes present in the sample and quantifies the relative amount of the target molecule for protein identification.

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This is a biosensor technique that is used in studying binding kinetics and affinity of molecular interactions. Choice between single- or multi-cycle kinetics is possible with the BiacoreTM X100 System.

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This analysis is widely used for studying the higher-order structure of biomacromolecules such as proteins, glycoproteins and DNA; subtle changes in the folding of the backbone can be detected in realistic aqueous environments by CD in the far-UV wavelength range.

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