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Detection of molten globule-like structure of proteins by Circular dichroism (CD) (CAT#: STEM-MB-0602-WXH)

Introduction

Molten globule is a stable, partially folded protein state found in mildly denaturing conditions such as low pH, mild denaturant or high temperature. Molten globules are collapsed and generally have some native-like secondary structure but a dynamic tertiary structure as seen by far and near circular dichroism spectroscopy, respectively. These traits are similar to those observed in the transient intermediate states found during the folding of certain proteins, especially globular proteins that undergo hydrophobic collapse, and therefore the term 'molten globule' is also used to refer to certain protein folding intermediates corresponding to the narrowing region of the folding funnel higher in energy than the native state but lower than the denatured state. The molten globule ensembles sampled during protein folding and unfolding are thought to be roughly similar.




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