Chemical unfolding (stability) studies of membrane proteins by Circular dichroism (CD) (CAT#: STEM-MB-0599-WXH)

Introduction

Chemical denaturants such as guanidine hydrochloride and urea are commonly used to assess the stability of either apo- versus ligand-bound soluble proteins, or the effects of mutations (both with and with ligands added). They may or may not be effective in unfolding membrane proteins, and must be tested on a case-by-case basis. If the unfolding transition is fully reversible, such studies have greater value as they can be used to determine thermodynamic parameters associated with the protein stability.