Looking at Human Cytosolic
Sialidase NEU2 Structural
Features with an Interdisciplinary Approach
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Abstract
Circular dichroism (CD) spectra at
variable temperatures have been
recorded for human cytosolic sialidase NEU2 in buffered water solutions
and in the presence of divalent cations. The results show the prevalence
of β-strands together with a considerable amount of α-helical
structure, while in the solid state, from both previous X-ray diffraction
analysis and our CD data on film samples, the content of β-strands
is higher. In solution, a significant change in CD spectra occurs
with an increase in temperature, related to a decrease in α-helix
content and a slight increase in β-strand content. In the same
range of temperatures, the enzymatic activity decreases. Although
the overall structure of the protein appears to be particularly stable,
molecular dynamics simulations performed at various temperatures evidence
local conformational changes possibly relevant for explaining the
relative lability of enzymatic activity