Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution
10 ppages.-- 8 figures.-- 1 table.-- PMID: 14710843 [PubMed].-- Printed version published Oct 15, 2003.
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| Format: | artículo biblioteca |
| Language: | English |
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American Chemical Society
2003-09-03
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| Subjects: | MIR, NIR, MCR−ALS, Protein structures, Multivariate Curve Resolution, |
| Online Access: | http://hdl.handle.net/10261/19381 |
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dig-idaea-es-10261-193812019-02-14T13:19:03Z Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution Navea, Susana Juan, Anna de Tauler, Romà MIR NIR MCR−ALS Protein structures Multivariate Curve Resolution 10 ppages.-- 8 figures.-- 1 table.-- PMID: 14710843 [PubMed].-- Printed version published Oct 15, 2003. The 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. Peer reviewed 2009-12-07T09:24:01Z 2009-12-07T09:24:01Z 2003-09-03 artículo http://purl.org/coar/resource_type/c_6501 Analytical Chemistry 75(20): 5592-5601 (2003) 0003-2700 http://hdl.handle.net/10261/19381 10.1021/ac0343883 1520-6882 en http://dx.doi.org/10.1021/ac0343883 none 22195 bytes application/pdf American Chemical Society |
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MIR NIR MCR−ALS Protein structures Multivariate Curve Resolution MIR NIR MCR−ALS Protein structures Multivariate Curve Resolution |
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MIR NIR MCR−ALS Protein structures Multivariate Curve Resolution MIR NIR MCR−ALS Protein structures Multivariate Curve Resolution Navea, Susana Juan, Anna de Tauler, Romà Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution |
| description |
10 ppages.-- 8 figures.-- 1 table.-- PMID: 14710843 [PubMed].-- Printed version published Oct 15, 2003. |
| format |
artículo |
| topic_facet |
MIR NIR MCR−ALS Protein structures Multivariate Curve Resolution |
| author |
Navea, Susana Juan, Anna de Tauler, Romà |
| author_facet |
Navea, Susana Juan, Anna de Tauler, Romà |
| author_sort |
Navea, Susana |
| title |
Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution |
| title_short |
Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution |
| title_full |
Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution |
| title_fullStr |
Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution |
| title_full_unstemmed |
Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution |
| title_sort |
modeling temperature-dependent protein structural transitions by combined near-ir and mid-ir spectroscopies and multivariate curve resolution |
| publisher |
American Chemical Society |
| publishDate |
2003-09-03 |
| url |
http://hdl.handle.net/10261/19381 |
| work_keys_str_mv |
AT naveasusana modelingtemperaturedependentproteinstructuraltransitionsbycombinednearirandmidirspectroscopiesandmultivariatecurveresolution AT juanannade modelingtemperaturedependentproteinstructuraltransitionsbycombinednearirandmidirspectroscopiesandmultivariatecurveresolution AT taulerroma modelingtemperaturedependentproteinstructuraltransitionsbycombinednearirandmidirspectroscopiesandmultivariatecurveresolution |
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1777669167007137792 |