CONFOCHECK
Answers about Protein Dynamics.
And Other Structural Parameters.
Secondary Structure Determination in Proteins using FT-IR
Main applications for the CONFOCHECK are the detection and quantification of conformational changes in proteins and the protein concentration determination. Quantitative determination of the protein concentration and the secondary structure elements (alpha-helix, beta-sheet) from the analyzed protein samples is accomplished within seconds via internal calibrations.
The CONFOCHECK is equipped with several specific protein sampling cuvettes that allow the measurement of solved and membrane bound proteins, even at very low amounts (10 µg). To reach optimal temperature constancy and to facilitate the measurement of temperature induced protein conformational changes, the sample cuvettes are temperature-controlled by a thermostat.
The Complete Protein Analysis Solution
FT-IR Protein Applications:
- Protein quantification
- Detection of conformational changes
- Protein dynamics (temperature induced conformational changes)
- Monitoring of conformational changes during protein aggregation, precipitation and crystallization
- Determination of the secondary structure
- Quantification of all kind of solutes in aqueous samples (buffers, excipients, detergents)
Analyzing Proteins in Pharma:
- Pre-formulation and formulation development: Analysis of the influence of the formulation on protein stability
- Stability studies (stress tests): Influence of pH, temperature, mutation, etc. on the protein stability
- Quality control: Check of protein concentration, structure on correct product composition (buffer, excipients) in production environment
- Binding studies: Analysis of the impact of ligand-binding on the protein structure
CONFOCHECK Benefits:
- Complete system can be validated to use in pharmaceutical quality control.
- Optimized, long-life components to minimize maintenance and prolong revalidation cycles.
- Gold optics for maximum sensitivity in the MIR
- 10 year warranty on laser
- 10 year warranty on interferometer
- 5 year warranty on MIR source
AquaSpec Transmission Cell
The AquaSpec™ is used for the measurement of water soluble proteins or solubilized membrane-bound proteins. Using the internal calibrations of the CONFOCHECK the secondary structure and concentration of the analyzed protein are determined directly after measurement (ca. 30 sec).
It features a flow-through transmission cell, with an optimal path length of ~7 µm. The AquaSpec™ also permits higher sample throughput and accuracy. Easily measure low protein concentrations (below 0.1 mg/ml) and detect the smallest conformational changes.
Using the AquaSpecTM transmission cell the highest sensitivity for the detection of conformational changes and the best accuracy in the protein concentration determination is achieved.
Applications
- Determination of changes in protein structure
- Protein concentration determination
- Quality control of biopharmaceuticals
- Secondary structure determination
- Quantification of various substances in aqueous solutions
BioATR II
The BioATR II is a micro-ATR unit that was specially developed for the investigation of temperature-induced unfolding, refolding and denaturation processes of proteins in aqueous media.
It can be applied for water solved and also for membrane-standing proteins. The number of internal reflections in the ATR crystal (silicon) is adjusted to result in an optimal protein signal in aqueous samples.
Applications:
- Automated temperature ramps (0-95°C):
- Analysis of temperature-induced conformational changes
- Measurement of phase transitions in lipids
- Quality control of biopharmaceuticals
- Membrane-standing proteins
- Conformational changes induced by ligand-binding, pH-changes, salts
The BioATR II is temperature-controlled by the same thermostat like the other accessories that are part of the CONFOCHECK system. With this unit temperature ramps from 0 to 95°C can be performed automatically to analyze the temperature-induced structural changes and the protein melting point.
Furthermore, you can characterize fibrillation and aggregation processes and monitor protein structural changes in dependence of pH‑changes or ligand-binding interactions. Using a special dialysis top section for BioATR II, low molecular weight substances can be dialyzed into the protein compartment without diluting the protein.
Literature Room
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