DOI | Trouver le DOI : https://doi.org/10.1063/1.1302851 |
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Auteur | Rechercher : Schultz, Christinan P.1; Rechercher : Bârzu, Octavian; Rechercher : Mantsch, Henry H.1 |
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Affiliation | - Conseil national de recherches du Canada. Institut du biodiagnostic du CNRC
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Format | Texte, Chapitre de livre |
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Conférence | Two-Dimensional Correlation Spectroscopy, August 29 - September 1, 1999, Kobe-Sanda, Japan |
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Sujet | enzymes; nucleotides; proteins; infrared spectra; secondary structure |
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Résumé | The functional role of CMP kinases is to regenerate mono-phosphate nucleotides in cells by transferring phosphate residues from tri-phosphorylated nucleotides to monophosphorylated nucleotides. These enzymes possess two binding sites and maintain a highly conserved secondary structure. They are essential for cell survival. Herein we compare the infrared spectra of two similar, but not identical enzymes, the CMP kinases from Escherichia coli and Bacillus subtilis. A two-dimensional cross correlation analysis of the infrared spectra reveals differences in the denaturation behavior of the two proteins. Different secondary structure elements show different time-delayed or advanced unfolding events in the two enzymes. When bound to the active sites, the two nucleotide-substrates CMP and ATP exert a stabilizing effect on the structure of both proteins. The changes observed upon thermal denaturation are different for the two enzymes. Model 2D correlations are used to simulate the different denaturation of the two enzymes. Thermal denaturation and aggregation can be distinguished as two processes separated in time. |
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Date de publication | 2000-03-10 |
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Maison d’édition | American Institute of Physics |
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Dans | |
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Série | |
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Publications évaluées par des pairs | Oui |
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Numéro du CNRC | NRC-IBD-1822 |
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Numéro NPARC | 9148476 |
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Exporter la notice | Exporter en format RIS |
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Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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Identificateur de l’enregistrement | 4cda896d-3d2b-4048-9be5-d05bdf355a8e |
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Enregistrement créé | 2009-06-25 |
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Enregistrement modifié | 2020-06-12 |
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