Two-dimensional; 1; H and; 1; H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields

Varghese, Sabu and Halling, Peter J. and Häussinger, Daniel and Wimperis, Stephen. (2018) Two-dimensional; 1; H and; 1; H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields. Solid state nuclear magnetic resonance, 92. pp. 7-11.

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Nuclear magnetic resonance (NMR) is a powerful tool for investigating atomic-scale structure in heterogeneous or composite materials where long-range order is absent. In this work solid-state; 1; H and; 1; H-detected NMR experiments were performed with fast magic angle spinning (ν; R; = 75 kHz) and at high magnetic fields (B; 0; = 20 T) and used to gain structural insight into a heterogeneous biocatalyst consisting of an enzyme, human carbonic anhydrase II (hCA II), covalently immobilized on epoxy-functionalized silica. Two-dimensional; 1; H-; 1; H NOESY-type correlation experiments were able to provide information on; 1; H environments in silica, epoxy-silica and the immobilized enzyme. Two distinct signals originating from water protons were observed: water associated with the surface of the silica and the water associated with the immobilized enzyme. Additional two-dimensional; 1; H-; 1; H double-single quantum (DQ-SQ) correlation experiments suggested that the immobilized enzyme is not in close contact with the silica surface. Most significantly, comparison of two-dimensional; 1; H-; 15; N spectra of the immobilized enzyme and the solution-state enzyme confirmed that the structural integrity of the protein is well preserved upon covalent immobilization.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Nuclear Magnetic Resonance (Häussinger)
UniBasel Contributors:Häussinger, Daniel
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:15 May 2019 08:43
Deposited On:15 May 2019 08:43

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