Identifying the interactions during protein refolding reactions by Dynamic light scattering (DLS) (CAT#: STEM-MB-0553-WXH)

Introduction

Protein folding is the physical process by which a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Protein refolding is a key step for large scale production of recombinant proteins. Solubilized/unfolded protein needs to be refolded into the correct conformation to obtain a biologically active form.

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Principle Applications Procedure Materials Notes Related Products

Principle

Dynamic Light Scattering (DLS) is an established and precise measurement technique for characterizing particle sizes in suspensions and emulsions. It is based on the Brownian motion of particles - this states that smaller particles move faster, while larger ones move slower in a liquid. The light scattered by particles contains information on the diffusion speed and thus on the size distribution.
The Dynamic Light Scattering (DLS) technique measures motion optically by recording the scattered light signal at a fixed angle. The particles are illuminated with a monochromatic, coherent light source (laser) and the light scattered by the particles is recorded.

Applications

DLS is used to characterize the size of various particles including proteins, polymers, micelles, Protein cages and virus-like particles, vesicles, carbohydrates, nanoparticles, biological cells, and gels.

Procedure

1. Sample preparation
2. Measurement by DLS instrument
3. Data analysis

Materials

• Dynamic Light Scattering (DLS) instruments (Photon Correlation Spectroscopy or Quasi-Elastic Light Scattering instruments)
• Dynamic Light Scattering Detector

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