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dc.contributor.authorNavea, Susana-
dc.contributor.authorJuan, Anna de-
dc.contributor.authorTauler, Romà-
dc.identifier.citationAnalytical Chemistry 75(20): 5592-5601 (2003)en_US
dc.description10 ppages.-- 8 figures.-- 1 table.-- PMID: 14710843 [PubMed].-- Printed version published Oct 15, 2003.en_US
dc.description.abstractThe combination of near- and midinfrared spectroscopies (NIR and MIR) is proposed to monitor temperature-dependent transitions of proteins. These techniques offer a high discriminating power to distinguish among protein structural conformations but, in temperature-dependent processes, present the drawback associated with the intense and evolving absorption of the deuterium oxide, used as a solvent in the protein solutions. Multivariate curve resolution−alternating least squares (MCR−ALS) is chosen as the data analysis technique able to unravel the contributions of the pure protein and deuterium oxide species from the mixed raw experimental measurements. To do so, MCR−ALS works by analyzing simultaneously experiments from MIR and NIR on pure deuterium oxide solutions and protein solutions in D2O. This strategy has proven to be effective for modeling the protein process in the presence of D2O and, therefore, for avoiding the inclusion of artifacts in the data stemming from inadequate baseline corrections. The use of MIR and NIR and MCR−ALS has been tested in the study of the temperature-dependent evolution of β-lactoglobulin. Only the combined use of these two infrared techniques has allowed for the distinction of the three pure conformations involved in the process in the working thermal range: native, R-type state, and molten globule.en_US
dc.format.extent22195 bytes-
dc.publisherAmerican Chemical Societyen_US
dc.subjectProtein structuresen_US
dc.subjectMultivariate Curve Resolutionen_US
dc.titleModeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolutionen_US
dc.description.peerreviewedPeer revieweden_US
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