NMR Proton Spin-Lattice Relaxation Mechanism in D2O Solutions of Albumin Determined at 400 MHz

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dc.contributor.authorYilmaz, A.
dc.contributor.authorZengin, B.
dc.contributor.authorUlak, F. Sadan
dc.date.accessioned2024-04-24T16:02:12Z
dc.date.available2024-04-24T16:02:12Z
dc.date.issued2014
dc.departmentDicle Üniversitesien_US
dc.description.abstractT-1 values in pure D2O and D2O solutions of human serum albumin (HSA) were measured versus temperature. A formula was derived based on H-H interactions between the surface HDO and non-exchangeable protein protons. The formula was used to evaluate the average distance of the interactions (rav). The effective correlation times were then derived by replacing the experimental data in the formula. Short correlation times obtained for the solution with low HSA (0.02 g albumin for one ml of D2O) decreased from 53 to 29 ps, while longer times increased from 1.19 to 2.22 ns. They are of the order of a fraction of a nanosecond for the solution with high HSA (0.08 g albumin per one ml of D2O). The perfect consistency between the derived theory and experimental data indicates that the high-field 1/T-1 in D2O solutions of albumin is caused by dipolar interactions between the surface HDO and non-exchangeable protein protons. It also suggests that the effective correlation time of the surface HDO is of the order of the mean lifetime of short-lived surface water.en_US
dc.identifier.doi10.1007/s10812-014-9938-1
dc.identifier.endpage370en_US
dc.identifier.issn0021-9037
dc.identifier.issn1573-8647
dc.identifier.issue3en_US
dc.identifier.scopus2-s2.0-84905573683en_US
dc.identifier.scopusqualityQ4en_US
dc.identifier.startpage365en_US
dc.identifier.urihttps://doi.org/10.1007/s10812-014-9938-1
dc.identifier.urihttps://hdl.handle.net/11468/14687
dc.identifier.volume81en_US
dc.identifier.wosWOS:000340500400003
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofJournal of Applied Spectroscopyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectProton Nmren_US
dc.subjectSurface Hdoen_US
dc.subjectAlbuminen_US
dc.titleNMR Proton Spin-Lattice Relaxation Mechanism in D2O Solutions of Albumin Determined at 400 MHzen_US
dc.typeArticleen_US

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