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Study of recombinant prion proteins (recPrP) structure by Circular dichroism (CD) (CAT#: STEM-MB-0617-WXH)

Introduction

The availability of recombinant prion proteins (recPrP) has been exploited as a model system to study PrP-mediated toxicity, conversion and infectivity. It has been hypothesized that the central event in the pathogenesis of prion diseases is the conversion of PrP(C) to PrP (Sc). This involves a dramatic increase in beta sheet conformation as PrP(C) is converted to PrP(Sc) and it is widely believed that this conformational change affects the undefined function of PrP(C).




Principle

Circular dichroism (CD) is a spectroscopy technique that measures the absorption difference between left and right circularly polarized light. By symmetry, this asymmetric absorption can only occur for asymmetric molecules, meaning chiral molecules.

Applications

Circular dichroism (CD) spectroscopy is a powerful technique that is sensitive to the chirality (handedness) of molecules. It can be used to study absolute stereochemistry, enantiomeric composition, racemization, enantiomeric differentiation, and molecular interactions and conformation.

Procedure

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

Materials

Circular dichroism (CD) spectrophotometer
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