Circular Dichroism Spectrophotometer (CD) J-1500, Jasco


Circular Dichroism Spectrophotometer (CD) J-1500, Jasco

Location:
CEITEC BUT

Research group:
Advanced Biomaterials - Lucy Vojtová


Circular Dichroism Spectrophotometer (CD) J-1500, Jasco

CD is a special subtype spectrophotometer UV-VIS facility which is able to measure the absorption spectrum and the CD spectrum. The CD spectrum is measured with circularly polarized light, and provides important information on the chiral molecules (part of the molecule is arranged in a helix). Much of the natural molecule is chiral and therefore exhibits the typical CD spectrum of the device can then identify changes in the secondary structure of these molecules. The device can thus observe how the molecule is arranged. For example, what type of molecule is measured, as well dissolves in the solvent as resistant to solvents and when the solvent starts to fall apart (denaturation), how it reacts to temperature changes as precipitation in the deterioration of the solvent (adding salt, etc..), or what is the reaction after adding crosslinker. The device has a major impact on research of natural polymers mainly of collagen.

Based on the principle of circular dichroism (CD) - difference in the absorption of left-handed circularly polarised light (L-CPL) and right-handed circularly polarised light (R-CPL)
Applicable for molecules containing one or more chiral chromophores (light-absorbing groups)
Measurements carried out in the visible and ultra-violet region of the electro-magnetic spectrum monitor electronic transitions, a circular dichroism signal can be positive or negative, depending on whether L-CPL is absorbed to a greater extent than R-CPL (CD signal positive) or to a lesser extent (CD signal negative)
Fast, quantitative and non-destructive photometric technique that is used extensively to study chiral molecules of all types and sizes
Analysis of bulky biological molecules with regard to their stability, structure and interactions of nucleic acids and proteins.

Use

Determination of protein secondary structure
Determination of optical purity
Analysis of the tertiary structure of proteins and conformational changes
Comparison of the secondary and tertiary structures of wild-type and mutant proteins
Binding studies involving conformational changes
Nucleic acid structure and changes upon binding or melting
Thermodynamic parameters from temperature dependencies of CD signals
Kinetics of conformational changes on msec timescales
Quantitative analysis of pharmaceuticals