CD spectra is a sensitive method to identify the conformational changes of protein [50].
Effector molecules bind at the protein's allosteric sites, leading to the changes of protein activity.
Notably, relative changes of protein quantity can be elucidated with the method applied here.
However, little information about the structural changes of protein hydrolysates is available.
In addition, the changes of protein abundance were analyzed by comparing the differences between high-yield and the background strain.
We described how the structural changes of protein were different and how water molecules were involved in them.
The binding difference between C60 and two proteins, the location of C60 nanoparticles and the changes of protein conformation and secondary structure were also proposed.
Their knockout/wild-type ratios indicate relative changes of protein acetylation levels in the livers of HDAC6 knockout mice vs. wild-type mice.
To determine if these changes of protein content were associated with alterations in gene expression, semi-quantitative reverse transcription polymerase chain reaction (RT-PCR) was performed.
These trends could be described by sigmoid models, which allowed determining onset temperatures for changes of protein solubility in the interval [125, 146 °C], whatever moisture content.
The conformational changes of protein secondary structure in the presence of above complex were demonstrated by FT-IR, three-dimensional fluorescence and UV Vis absorption techniques.
