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.
- Dynamic Light Scattering.
- X-ray Crystallography.
- Research collaboration.
- 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.