Home > Biophysics characterisation > Circular Dichroism > Circular Dichroism
Presentation CDPresentationStudying macromolecules (and in particular proteins) by circular dichroism allows to obtain information about their folding. Circular dichroism (CD) spectroscopy measures differences in the absorption of left-handed polarized light versus right-handed polarized light which arise due to structural asymmetry. For proteins, far UV (180-260 nm) and near UV (250-330 nm) circular dichroism measurements give insight respectively into their secondary structure content and their tertiary organization. CD is particularly useful for monitoring changes in structure upon ligand binding or changes to the protein’s environment. Thermal stability of folded molecules can be determined by performing temperature gradient to the sample. Similarly, conformational stability of a molecule and structural changes induced by complex formation can be checked at constant temperature by adding step by step chemical denaturation agents. Application
Key wordsSecondary structure, tertiary organization, Interactions, Kinetics of folding and unfolding StaffManager: Caroline Mas Specific EquipmentAccess modeUsers must read the conditions of use of the instruments as well as of the management of the services provided: Instrument allocation after user training:
CostAcademics: Participation to the maintenance fees LocationThe Biophysical platform is located in the Carl-Ivar Brändén Building, ground floor, room 001 (Shared Building C). How to make a requestTo make a booking request, fill this request form here CD BookingSamplesOnly non-pathogenic biological samples are accepted. Decree of the July 18, 1994 establishing the list of biological pathogens, amended by Decrees of April 17, 1997 and June 30, 1998 (Decrees in French). The list of biological pathogens is available on the website of the IPBS.
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