Circular Dichroism Spectroscopy

St Vincent


Ms. Belinda Michell

(613) 9228 2480

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Post author: Belinda Michell. Last update: 02/11/2015 at 2:43 pm by Belinda Michell.


The CD spectromometer shines polarised light at proteins and allows analysis of protein secondary structure from circular dichroism spectra – for example a-helices and ß-sheets (far UV spectrum) – and aids monitoring of protein folding and conformational changes prior to using more expensive and time consuming methods such as NMR and X-ray crystallography. Secondary structure can be determined by CD spectroscopy in the “far-uv” spectral region. Thermal stability can be assessed using CD by following changes in the spectrum with increasing temperature. CD gives less specific structural information than X-ray crystallography and protein NMR spectroscopy, for example, which both give atomic resolution data. However, CD spectroscopy is a quick method that does not require large amounts of proteins or extensive data processing.

Other infrastructure:

  • Dynamic Light Scattering.
  • X-ray Crystallography.

Access by:

  • Research collaboration.



Know how:

  • Circular dichroism.

Expertise:Availability of technical support:

  • Support for instrument use is available.

Note that this material was imported form the Victorian Bioportal and content requires updating.


CD Spectrometer

ircular Dichroism spectroscopy measuring in the UV/Vis (163-900nm) spectrum used for A very straightforward, accessible technique to investigate the secondary structure of proteins.

Facility: |


Circular Dichroism Spectroscopy

St Vincent’s Institute of Medical Research, . 9 Princes Street, Fitzroy, Victoria, Australia.

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Type: Core facility in a research organisation
Discipline areas: Biological Science
Precinct: Central
Affiliations: St Vincents Institute of Medical Research

Biological Science categories: NMR and CD spectroscopy, Structural biology