Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Mariella Parisi"'
Publikováno v:
Journal of Structural Biology. 159:82-91
Dissociation of bovine odorant binding protein (bOBP) dimers to monomers at pH 2.5 has been confirmed through size exclusion chromatography experiments. Moreover, structural and binding properties of the acidic monomer and neutral dimer have been com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f548c2237c24684006be570c04e5cc3b
https://doi.org/10.1016/j.jsb.2007.02.007
https://doi.org/10.1016/j.jsb.2007.02.007
Autor:
Mariella Parisi, Roberto Ramoni, Roberto Favilla, Stefano Grolli, Alberto Mazzini, R. T. Sorbi
Publikováno v:
Biochimica et biophysica acta. 1750(1)
Porcine odorant binding protein (pOBP) contains a single disulphide bridge linking residues Cys63 and Cys155. In order to get information on the role played by this crosslink in determining the structural and functional properties of the protein, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69a5fa1638d3c7905f857be1d314b7e6
https://pubmed.ncbi.nlm.nih.gov/15886077
https://pubmed.ncbi.nlm.nih.gov/15886077
Autor:
Roberto Favilla, Mariella Parisi, Alberto Mazzini, Roberto Ramoni, Stefano Grolli, R. T. Sorbi
Publikováno v:
Biochimica et biophysica acta. 1652(2)
Unfolding and refolding studies on porcine odorant binding protein (pOBP) have been performed at pH 7 in the presence of guanidinium hydrochloride (GdnHCl). Unfolding, monitored by following changes of protein fluorescence and circular dichroism (CD)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b912a1ed191d6a22afea07a95d1e266
https://pubmed.ncbi.nlm.nih.gov/14644047
https://pubmed.ncbi.nlm.nih.gov/14644047
Autor:
Roberto Favilla, Roberto Ramoni, Mariella Parisi, R. T. Sorbi, Alessia Maia, Alberto Mazzini, Stefano Grolli
Publikováno v:
Biochimica et biophysica acta. 1599(1-2)
An analysis of the unfolding and refolding curves at equilibrium of dimeric bovine odorant binding protein (bOBP) has been performed. Unfolding induced by guanidinium chloride (GdnHCl) is completely reversible as far as structure and ligand binding c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee36d2a93aa6e6d1be4c0522515a0aeb
https://pubmed.ncbi.nlm.nih.gov/12479409
https://pubmed.ncbi.nlm.nih.gov/12479409