Dissociation and unfolding of bovine odorant binding protein at acidic pH

Autor: Mariella Parisi, Roberto Favilla, Alberto Mazzini, Eugenia Polverini, R. T. Sorbi

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

Dissociation kinetics of hemocyanin from Octopus vulgaris

Autor: Enrico Dainese, Benedetto Salvato, Mariano Beltramini, Roberto Favilla, Fabio Del Signore

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1385:115-125

The native form of hemocyanin (Hc) from Octopus vulgaris can be completely dissociated, at alkaline pH and in the presence of EDTA, from 49S decamers to 11S monomers. The kinetics of this process was studied, using a Bio-Logic stopped flow system, by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69182dc761fea58da5c7a92a33a6a6e9
https://doi.org/10.1016/s0167-4838(98)00037-5

Interaction of DAPI with pepsin as a function of pH and ionic strength

Autor: Roberto Favilla, Alberto Mazzini, Maddalena Incerti

Publikováno v: Biophysical Chemistry. 67:65-74

The fluorescent probe 4',6-diamidino-2-phenylindole (DAPI), extensively used with nucleic acids, has also recently been used with membranes and proteins (Favilla et al., Biophys. Chem., 46 (1993) 217-226 and Mazzini et al., Biophys. Chem. 52 (1994) 1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fe2985cff205f5152c38826d5553823
https://doi.org/10.1016/s0301-4622(97)00015-x

Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein

Autor: Paolo Lardi, Roberto Favilla, Conti Virna, Alberto Mazzini, R. T. Sorbi, Eugenia Polverini, Roberto Ramoni

Publikováno v: International Journal of Molecular Sciences
Volume 12
Issue 4
Pages 2294-2314
International Journal of Molecular Sciences, Vol 12, Iss 4, Pp 2294-2314 (2011)

The stability and functionality of GCC-bOBP, a monomeric triple mutant of bovine odorant binding protein, was investigated, in the presence of denaturant and in acidic pH conditions, by both protein and 1-aminoanthracene ligand fluorescence measureme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e7d1f18e00929bd7097c70eac2cbace

Fluorescence studies on the conformation of litorin in solution and in the presence of model membranes

Autor: Alberto Mazzini, Lorella Franzoni, Paolo Cavatorta, Alberto Spisni, Arthur G. Szabo, Roberto Favilla

Publikováno v: Journal of Fluorescence. 3:211-214

The conformation of the nonapeptide hormone litorin has been studied in buffer and in the presence of lipids, using static and dynamic fluorescence. The results obtained show that, in buffer, the hormone probably exists in a collection of flexible co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3723a861c848426650b84e55498f93dd
https://doi.org/10.1007/bf00865263