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Analysis of protein tertiary structure by Circular dichroism (CD) (CAT#: STEM-MB-0597-WXH)

Introduction

The CD spectrum of a protein in the 'near-UV' spectral region (250– 320 nm) can be sensitive to certain aspects of tertiary structure. At these wavelengths, the chromophores are the aromatic amino acids and disulfide bonds, and the CD signals they produce are sensitive to the overall tertiary structure of the protein. The near UV CD spectrum of a protein provides a valuable fingerprint of the tertiary structure of that protein, which can be used to compare, for example, wild type and mutant forms of proteins.




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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