Proteins in concentrated solutions behave like colloidal system whose interaction potential can be finely tuned by changing temperature, pH, salt content and ion species. An anion-driven formation of protein clusters has been encountered eventually evolving in a structural arrested state as testified by both the appearance of a low Q peak in the small angle neutron scattering spectra and a strong increase in the relative viscosity of the samples. These phenomena, taken together, can be considered as the signature of a gelation process that specifically depends on the nature of anions, according to the Hofmeister series.
Gelation in Cytochrome C concentrated solutions near the isoelectric point: the anion role / P. BAGLIONI; FRATINI E.; LONETTI B.; CHEN S. H.. - In: CURRENT OPINION IN COLLOID & INTERFACE SCIENCE. - ISSN 1359-0294. - STAMPA. - 9:(2004), pp. 38-42. [10.1016/j.cocis.2004.06.003]
Gelation in Cytochrome C concentrated solutions near the isoelectric point: the anion role
BAGLIONI, PIERO;FRATINI, EMILIANO;LONETTI, BARBARA;
2004
Abstract
Proteins in concentrated solutions behave like colloidal system whose interaction potential can be finely tuned by changing temperature, pH, salt content and ion species. An anion-driven formation of protein clusters has been encountered eventually evolving in a structural arrested state as testified by both the appearance of a low Q peak in the small angle neutron scattering spectra and a strong increase in the relative viscosity of the samples. These phenomena, taken together, can be considered as the signature of a gelation process that specifically depends on the nature of anions, according to the Hofmeister series.
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