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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Monti E,Benaglia G,Mozzi A,Fusi P,Longhi G,Gangemi F,Castiglioni E,Woody RW,Fornili SL,Abbate Sdoi
10.1021/bi500249rsubject
Has Abstractpub_date
2014-08-19 00:00:00pages
5343-55issue
32eissn
0006-2960issn
1520-4995journal_volume
53pub_type
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