Effect of electrostatic energy on partitioning of proteins in aqueous two-phase systems

dc.creatorOlivera Nappa, Álvaro
dc.creatorLagomarsino, G.
dc.creatorAndrews Farrow, Bárbara
dc.creatorAsenjo de Leuze, Juan
dc.date.accessioned2007-05-07T16:22:10Z
dc.date.available2007-05-07T16:22:10Z
dc.date.created2007-05-07T16:22:10Z
dc.date.issued2004-07-25
dc.identifierJOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES 807 (1): 81-86 JUL 25 2004
dc.identifier1570-0232
dc.identifierhttps://repositorio.uchile.cl/handle/2250/124555
dc.description.abstractAn attempt has been made to adopt a different approach to evaluate the effect of a protein's charge on its partitioning behaviour in PEG/salt aqueous two-phase systems (ATPS). This has been done using a computer methodology (DelPhi) that allows the calculation of the electrostatic solvation energy that charged proteins present in a particular media such as aqueous polymer-salt systems. This calculation was done for the protein in each of the phases and a correlation was investigated that related the electrostatic energy difference of the protein in each of the phases and its partition coefficient in ATPS. Such correlation resulted in a statistical model that also included the effect of molecular weight and a shape factor at each particular pH. A global correlation which included the effect of pH was also found. All the correlations were statistically evaluated and gave good results.
dc.languageen
dc.publisherELSEVIER
dc.subjectCHEMICALLY-MODIFIED PROTEINS
dc.titleEffect of electrostatic energy on partitioning of proteins in aqueous two-phase systems
dc.typeArtículo de revista


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