A method for determining states in the course of protein unfolding

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dc.contributor.authorMahdavi, Seyed Mohammadde
dc.contributor.authorMarashi, Sayed-Amirde
dc.contributor.authorRezaei-Tavirani, Mostafade
dc.date.accessioned2008-06-17T14:05:43Z
dc.date.available2008-06-17T14:05:43Z
dc.date.issued2006-09-27de
dc.description.abstractA simple model is presented for analyzing a set of spectra obtained from spectrophotometric study of protein titration. With this model one can determine the states of (probable) intermediates in the course of protein unfolding. The model is developed based on abundance of native state, intermediate(s) and denatured state, and their contributions to differential absorbance at selected wavelengths. The model is tested for the two-state unfolding of ribonuclease A by urea in formate buffer, and also for the three-state unfolding of a-lactalbumin by guanidine hydrochloride (GdnHCl) in phosphate buffer. It was demonstrated that unfolding of ribonuclease A is matched acceptably with the two-state model, while a-lactalbumin unfolding starts with a two-state mechanism (when [GdnHCl]>=1.6M) followed by a three-state pathway.en
dc.identifier.issn1611-2156de
dc.identifier.urihttp://hdl.handle.net/2003/25669
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-122
dc.language.isoende
dc.relation.ispartofseriesEXCLI Journal ; Vol. 5, 2006en
dc.subjectalpha-lactalbuminen
dc.subjectribonuclease Aen
dc.subjectrotein denaturationen
dc.subjectspectrophotometryen
dc.subjectthree-state denaturationen
dc.subjecttwo-state denaturationen
dc.subject.ddc610
dc.titleA method for determining states in the course of protein unfoldingen
dc.typeTextde
dc.type.publicationtypearticlede
dcterms.accessRightsopen access
eldorado.dnb.zdberstkatid2132560-1

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