title: Looking at human cytosolic sialidase NEU2 structural features with an interdisciplinary approach.
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.
authors.affiliation: Department of Molecular and Translational Medicine (DMTM), University of Brescia , Viale Europa 11, 25123 Brescia, Italy.
authors.forename: Eugenio
authors.initials: E
authors.lastname: Monti
authors.forename: Giuliana
authors.initials: G
authors.lastname: Benaglia
authors.forename: Alessandra
authors.initials: A
authors.lastname: Mozzi
authors.forename: Paola
authors.initials: P
authors.lastname: Fusi
authors.forename: Giovanna
authors.initials: G
authors.lastname: Longhi
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Gangemi
authors.forename: Ettore
authors.initials: E
authors.lastname: Castiglioni
authors.forename: Robert W
authors.initials: RW
authors.lastname: Woody
authors.forename: Sandro L
authors.initials: SL
authors.lastname: Fornili
authors.forename: Sergio
authors.initials: S
authors.lastname: Abbate
mesh_terms: D002942:Circular Dichroism; D003198:Computer Simulation; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009439:Neuraminidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
chemical_list: C403285:NEU2 protein, human; D009439:Neuraminidase