Manipulation of a cation-π sandwich reveals conformational flexibility in phenylalanine hydroxylase

Fe3O4@SiO2@NiAl-LDH microspheres implication in separation, kinetic and structural properties of phenylalanine dehydrogenase

“…It seems that microspheres can cause a change in the tertiary structure of the protein. Previous studies have revealed that the change in the environment of Trp120, which is located between regulatory and catalytic domains, can cause a change in the intensity of fluorescence spectroscopy [ 92 ]. Also, a similar phenomenon was observed in published work on the assessment of the tertiary structure changes by analyzing the intrinsic fluorescence of mutant and native phenylalanine dehydrogenase obtained from Bacillus badius , have shown that change in the emission spectrum resulting from tyrosine can be a response to local changes around the indole ring of tyrosine and the mutant proteins show less fluorescence emission at 340 which was attributed to conformational changes of protein structure [ 93 ].…”