title: Impact of globule unfolding on dilational viscoelasticity of beta-lactoglobulin adsorption layers.
abstract: The dynamic surface dilational elasticity, surface pressure, and adsorbed amount of the mixed solutions of beta-lactoglobulin and guanidine hydrochloride were measured as a function of surface age and denaturant concentration. It was shown that the conformational transition from compact globules to disordered protein molecules in the surface layer leads to strong changes in the surface elasticity kinetic dependencies and thereby can be easily detected by measuring the surface dilational rheological properties. The corresponding changes of the kinetic dependencies of the surface pressure and adsorbed amount are not so pronounced but correlate with the results on surface dilational elasticity.
authors.affiliation: St. Petersburg State University, Chemical Faculty, 198904 St. Petersburg, Russia.
authors.forename: B A
authors.initials: BA
authors.lastname: Noskov
authors.forename: D O
authors.initials: DO
authors.lastname: Grigoriev
authors.forename: A V
authors.initials: AV
authors.lastname: Latnikova
authors.forename: S-Y
authors.initials: SY
authors.lastname: Lin
authors.forename: G
authors.initials: G
authors.lastname: Loglio
authors.forename: R
authors.initials: R
authors.lastname: Miller
mesh_terms: D000327:Adsorption; D004548:Elasticity; D019791:Guanidine / Q000737:chemistry; D007782:Lactoglobulins / Q000737:chemistry*; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D013499:Surface Properties; D014783:Viscosity
chemical_list: D007782:Lactoglobulins; D019791:Guanidine