BeStSel CFR program
Recently, Micsonai et al. developed the BeStSel algorithm that can accurately estimate the secondary structure composition from the CD spectrum by taking into account the parallel-antiparallel orientation of the β-strands and the twist of the antiparallel β-sheets. Spectra Manager™ 2.5 CFR BeStSel offers a control and analysis platform for CD spectrometers, which is compatible with GxP and satisfying computer system validation (CSV), electronic record/electronic signature (ER/ES), and data integrity (DI) for practice ALCOA+.
This BeStSel CFR is the dedicated commercial software of JASCO Spectra Manager.
If you have any question about this product or quotation request, please kindly contact our JASCO regional sales representatives.
Thermal denaturation analysis of monoclonal antibody
The advantage of BeStSel is not only its high accuracy in analyzing β-structure-rich-proteins, but also its feature of being able to calculate the fraction of eight secondary structure elements, including three types of twisting in antiparallel β-sheets.
Twisting of β-strand
As assessment examples by using BeStSel, the detailed secondary structure changes as a function of temperature were monitored. There is a significant difference between Herceptin® and h-IgG in changes in the distorted α-helix, left-twisted β-strand, relaxed β-strand and right-twisted β-strand. At 30 °C, h-IgG and Herceptin® have a similar secondary structure, but it was found that they have different denaturation mechanisms by using BeStSel. BeStSel is shown to be useful in understanding the detailed mechanisms of structure formation in proteins, including therapeutic antibodies.
Results of secondary structure prediction using BeStSel
Predicted secondary structure fraction of a) disordered Helix, b) left-twisted, c) relaxed, and d) right-twisted β-strand of Herceptin® (red) and human IgG (blue).
If you are interested in the on-line version of BeStSel software, please go to the following BeStSel web site at ELTE Eötvös Loránd University.