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Estimation of protein secondary structure by Circular dichroism (CD) (CAT#: STEM-MB-0596-WXH)

Introduction

Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. The secondary structure is an important level in the hierarchical classification of protein structure and it is used to identify protein features for fold recognition. Secondary structure is very important to protein in the evolution, size and geometry selection of the secondary structure motifs.




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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