AJUNTAMENT D'ALCOI
Website
Generalitat Valenciana
Website
Ayuntamiento de Valencia
Website
Cicloplast
Website
Ayuntamiento de Onil
Website
Anarpla
Website
Ayuntamiento de Mislata
Website
nlWA, North London Waste Authority
Website
Ayuntamiento de Salinas
Website
Zicla
Website
Fondazione Ecosistemi
Website
PEFC
Website
ALQUIENVAS
Website
DIPUTACI� DE VAL�NCIA
Website
AYUNTAMIENTO DE REQUENA
Website
UNIVERSIDAD DE ZARAGOZA
Website
OBSERVATORIO CONTRATACIÓN PÚBLICA
Website
AYUNTAMIENTO DE PAIPORTA
Website
AYUNTAMIENTO DE CUENCA
Website
BERL� S.A.
Website
CM PLASTIK
Website
TRANSFORMADORES INDUSTRIALES ECOL�GICOS
INDUSTRIAS AGAPITO
Website
RUBI KANGURO
Website
If you want to support our LIFE project as a STAKEHOLDER, please contact with us: life-future-project@aimplas.es
In this section, you can access to the latest technical information related to the FUTURE project topic.
Conformational changes of adsorbed and free proteins on magnetic nanoclusters
Conformational changes of proteins have an influence on their biological activity, so as to affect their use efficiency. However, the conformation of proteins is typically measured in a mixture containing the adsorbed protein, free protein and adsorbing material, which does not truly reflect the influence of the material on protein conformation. In this study, Fe3O4/carboxymethylated chitosan (Fe3O4/CMCS) nanoclusters with unique superparamagnetism were utilized as the separation carrier to study the conformational changes of the adsorbed and the free proteins. Four representative proteins with different molecular weights and isoelectric points, lysozyme (LYZ, 13.4?kDa; pI 10.8), bovine hemoglobin (BHB, 64.5?kDa; pI 6.9), apo-transferrin (TRT, 80?kDa; pI 5.9) and bovine serum albumin (BSA, 68?kDa; pI 4.8), were selected as model proteins to investigate the influences of material coating with/without metal ions and environmental factors including pH and ion strength, on the conformational behaviors of the adsorbed or free proteins. This study was aimed at providing a platform for an improved reflection of the conformational changes of proteins and has a potential to guide immobilization and separation of proteins.
» Author: Qi Yang, Bin Luo, Yue Zhu, Fang Lan, Yao Wu, Zhongwei Gu
» Reference: 10.1016/j.colsurfb.2018.05.056
» Publication Date: 01/10/2018
C/ Gustave Eiffel, 4
(València Parc Tecnològic) - 46980
PATERNA (Valencia) - SPAIN
(+34) 96 136 60 40
Project Management department - Sustainability and Industrial Recovery
life-future-project@aimplas.es