Circular Dichroism Spectrometer

Vienna Biocenter Core Facilities GmbH (VBCF)

Wien | Website

Large equipment

Short Description

Chirascan Plus CD spectrometer from Applied Photophysics

http://www.photophysics.com/products/chirascan-plus-cd-spectrometer

Contact Person

Peggy Stolt-Bergner

Research Services

The CD spectrum of a protein collected in the far-UV wavelength range (180 – 260 nm) reveals details of the secondary structure content. This information can be used to study the influence of point mutations on protein structure, to compare structural changes in the presence of ligands, or to ensure reproducibility and consistency between different protein batches, for example.

CD spectra in the near-UV wavelength range (230-350 nm) can also be used to study tertiary structural changes due to changes in the aromatic residues Tryptophan and Tyrosine in this wavelength range.

In addition CD can be used to study protein stability using thermal melt analysis to determine protein melting temperatures (Tm’s). Such experiments can be used to compare the stability of different protein mutants or to compare the stability of the same protein under different buffer conditions or in the presence of different ligands.

All of our CD data is collected on our Chirascan Plus CD spectrometer from Applied Photophysics. Experiments can be carried out for you, or alternatively you may receive training and can then book the instrument yourself.

Methods & Expertise for Research Infrastructure

The CD spectrum of a protein collected in the far-UV wavelength range (180 – 260 nm) reveals details of the secondary structure content. This information can be used to study the influence of point mutations on protein structure, to compare structural changes in the presence of ligands, or to ensure reproducibility and consistency between different protein batches, for example.

CD spectra in the near-UV wavelength range (230-350 nm) can also be used to study tertiary structural changes due to changes in the aromatic residues Tryptophan and Tyrosine in this wavelength range.

In addition CD can be used to study protein stability using thermal melt analysis to determine protein melting temperatures (Tm’s). Such experiments can be used to compare the stability of different protein mutants or to compare the stability of the same protein under different buffer conditions or in the presence of different ligands.

Allocation to Core Facility

Protein Technologies

Peggy Stolt-Bergner
Vienna Biocenter Core Facilities (VBCF)
+43 1 7962324 7070
peggy.stolt@vbcf.ac.at
http://www.vbcf.ac.at/protech
The Vienna Biocenter Core Facilities (VBCF) is a research institute providing access to state of the art infrastructure and advanced research services on a fee-for-service basis. Additionally, VBCF core facilities are open to all forms of scientific cooperation. Information on general conditions of cooperation and usage fees is provided upon request.