Zobrazeno 1 - 10
of 101
pro vyhledávání: '"Luigi Sportelli"'
Autor:
Andrea Stirpe, Rita Guzzi, Rosa Bartucci, Bruno Rizzuti, Maria Penelope De Santo, Luigi Sportelli, Manuela Pantusa
Publikováno v:
International Journal of Biological Macromolecules. 92:1049-1056
Several phenolic compounds bind to proteins and show the ability to interfere with their aggregation process. The impact of the natural polyphenol resveratrol on the stability and heat induced aggregation of human serum albumin (HSA) was investigated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9e66b137659239817393f086454ca23
https://doi.org/10.1016/j.ijbiomac.2016.08.014
https://doi.org/10.1016/j.ijbiomac.2016.08.014
Publikováno v:
Archives of Biochemistry and Biophysics. 579:18-25
Multiple molecular dynamics simulations were performed to investigate the association of stearic acid into the highest affinity binding site of human serum albumin. All binding events ended with a rapid (10 ps) lock-in of the fatty acid due to format
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f91c9be2e4c2c7fe668597043b47800
https://doi.org/10.1016/j.abb.2015.05.018
https://doi.org/10.1016/j.abb.2015.05.018
Publikováno v:
European Biophysics Journal. 41:969-977
The interaction between the natural polyphenol resveratrol and human serum albumin (HSA), the most abundant transport protein in plasma, has been studied in the absence and in the presence of up to six molecules of stearic acids (SA) pre-complexed wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db568383900df45f02b2dd17625c8e75
https://doi.org/10.1007/s00249-012-0856-y
https://doi.org/10.1007/s00249-012-0856-y
Autor:
Luigi Sportelli, Chan Li, Sachiko Yanagisawa, Christopher Dennison, Dorota Kostrz, Rita Guzzi
Publikováno v:
Archives of Biochemistry and Biophysics. 521:18-23
The copper site and overall structures of azurin (AZ) variants in which the amicyanin (AMI) and plastocyanin (PC) metal binding loops have been introduced, AZAMI and AZPC, respectively, are similar to that of AZ, whereas the loop conformations resemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7a8d5a9e3c5a8b71234e8ffabdab438
https://doi.org/10.1016/j.abb.2012.03.007
https://doi.org/10.1016/j.abb.2012.03.007
Publikováno v:
European Biophysics Journal. 40:273-279
Two-pulse, echo-detected electron paramagnetic resonance (ED-EPR) spectra and continuous-wave EPR (CW-EPR) spectra were used to investigate the solvent effect on the librational motion of human haemoglobin spin-labelled on cysteine β93 with the nitr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca86590fa7a0da82dc95a9e1eb21c328
https://doi.org/10.1007/s00249-010-0644-5
https://doi.org/10.1007/s00249-010-0644-5
Publikováno v:
Food Chemistry. 119:533-538
Antioxidant activity is displayed by amino acids, such as tryptophan (Trp), tyrosine (Tyr) and histidine (His) in the spontaneous oxidation of linoleic acid (LA). In addition, when Trp was incubated with soybean lipoxygenase (LOX 1) and LA, a modulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::978934f13071d2c0c1017c22749aaff4
https://doi.org/10.1016/j.foodchem.2009.06.065
https://doi.org/10.1016/j.foodchem.2009.06.065
Publikováno v:
Guzzi, R, Bartucci, R, Sportelli, L, Esmann, M & Marsh, D 2009, ' Conformational Heterogeneity and Spin-Labeled-SH Groups: Pulsed EPR of Na,K-ATPase ', Biochemistry, vol. 48, pp. 8343-8354 .
Membranous Na,K-ATPase from shark salt gland and from pig kidney was spin-labeled on class I -SH groups in the presence of glycerol, or on class II -SH groups in the absence of glycerol. The class I-labeled preparations retain full enzymatic activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73f3ab9a7e4ea52fc9ede10a582a69a2
https://doi.org/10.1021/bi900849z
https://doi.org/10.1021/bi900849z
Publikováno v:
European Biophysics Journal. 39:921-927
Electron spin resonance (ESR) spectroscopy is used to study the transfer of stearic acids between human serum albumin (HSA) and sterically stabilized liposomes (SSL) composed of dipalmitoylphosphatidylcholine (DPPC) and of submicellar content of poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8132e47a3a9d94c42f79bed6ae6dfa4a
https://doi.org/10.1007/s00249-009-0442-0
https://doi.org/10.1007/s00249-009-0442-0
Publikováno v:
Proteins
74 (2009): 961–971. doi:10.1002/prot.22204
info:cnr-pdr/source/autori:Rizzuti Bruno (1); Sportelli Luigi (2); Guzzi Rita (2)/titolo:Molecular dynamics of amicyanin reveals a conserved dynamical core for blue copper proteins/doi:10.1002%2Fprot.22204/rivista:Proteins (Print)/anno:2009/pagina_da:961/pagina_a:971/intervallo_pagine:961–971/volume:74
74 (2009): 961–971. doi:10.1002/prot.22204
info:cnr-pdr/source/autori:Rizzuti Bruno (1); Sportelli Luigi (2); Guzzi Rita (2)/titolo:Molecular dynamics of amicyanin reveals a conserved dynamical core for blue copper proteins/doi:10.1002%2Fprot.22204/rivista:Proteins (Print)/anno:2009/pagina_da:961/pagina_a:971/intervallo_pagine:961–971/volume:74
Molecular dynamics simulation has been carried out for the blue copper protein amicyanin from two different sources, Paracoccus denitrificans and Paraccocus versutus, to investigate the structural and dynamical properties common to the two molecules
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::388514848e84264497cb5301ce88230f
https://doi.org/10.1002/prot.22204
https://doi.org/10.1002/prot.22204
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784:1997-2003
The thermal stability of umecyanin, a stellacyanin from horseradish roots, has been investigated by differential scanning calorimetry, optical absorption and fluorescence spectroscopy at neutral and alkaline pH. Above pH 9 the Cu(II) protein experien
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efd51f05ae27d9a539dfa2b9899314d9
https://doi.org/10.1016/j.bbapap.2008.07.005
https://doi.org/10.1016/j.bbapap.2008.07.005