feature
All protein based drug formulations need freeze drying or spray drying. Modern research has shown that freeze-drying often leads to protein unfolding.

Folding of natural structures can lead to incomplete recovery of activity and unstable storage of polymers.
These issues usually require tedious and time-consuming activity measurements and detailed structural analysis to identify. Infrared spectroscopy technology is considered a fast, labor-saving, accurate, and reliable technique for determining the secondary structure of proteins. It is the only spectroscopic technique that can be used for solid analysis,
For example, regular powders, freeze-dried powders, fibers, ground powders, etc,
Can directly compare formula drugs with natural substances. This analyzer is equipped with specialized software for protein analysis, which can quickly compare the differences between natural structures and formulated proteins. The algorithm is composed of
Developed by Professor John Carpenter of the University of Colorado, or quantitatively determined through a built-in spectral database.
This database includes Fourier transform infrared spectra of the secondary structures of 50 known proteins, obtained under strictly controlled conditions and consistent with the structures measured by crystallization methods. It is the largest commercially available protein infrared database. Prota protein analyzer hardware includes: ABB

Bomem MB-104 Fourier transform infrared spectrometer, Pentium processor, calcium fluoride liquid sample tank, sample cleaning component.
parameter
Dry sample compartment with farsightedness cleaning tube capable of reverse flow cleaning
Moisture resistant ZnSe spectral prism

High sensitivity DTGS detector
Resolution: 1 cm-1-128 cm-1
Spectral range: 6500~500 cm-1
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