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    Rights statement: This is the author’s version of a work that was accepted for publication in Solid State Nuclear Magnetic Resonance. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Solid State Nuclear Magnetic Resonance, 92, 2018 DOI: 10.1016/j.ssnmr.2018.03.003

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

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Two-dimensional 1H and 1H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields. / Varghese, Sabu; Halling, Peter J.; Häussinger, Daniel et al.
In: Solid State Nuclear Magnetic Resonance, Vol. 92, 08.2018, p. 7-11.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

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Varghese S, Halling PJ, Häussinger D, Wimperis S. Two-dimensional 1H and 1H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields. Solid State Nuclear Magnetic Resonance. 2018 Aug;92:7-11. Epub 2018 Mar 14. doi: 10.1016/j.ssnmr.2018.03.003

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Varghese, Sabu ; Halling, Peter J. ; Häussinger, Daniel et al. / Two-dimensional 1H and 1H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields. In: Solid State Nuclear Magnetic Resonance. 2018 ; Vol. 92. pp. 7-11.

Bibtex

@article{a53a03d5db46482a97d356d720598b37,
title = "Two-dimensional 1H and 1H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields",
abstract = "Abstract 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 1H and 1H-detected NMR experiments were performed with fast magic angle spinning (νR = 75 kHz) and at high magnetic fields (B0 = 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 1H-1H NOESY-type correlation experiments were able to provide information on 1H 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 1H-1H 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 1H-15N spectra of the immobilized enzyme and the solution-state enzyme confirmed that the structural integrity of the protein is well preserved upon covalent immobilization.",
keywords = "Immobilized enzymes, Heterogeneous biocatalysts, Solid-state NMR, Biocatalysis, 1H MAS NMR, Epoxy-functionalized silica, Human carbonic anhydrase II, hCA II, Covalent immobilization",
author = "Sabu Varghese and Halling, {Peter J.} and Daniel H{\"a}ussinger and Stephen Wimperis",
note = "This is the author{\textquoteright}s version of a work that was accepted for publication in Solid State Nuclear Magnetic Resonance. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Solid State Nuclear Magnetic Resonance, 92, 2018 DOI: 10.1016/j.ssnmr.2018.03.003",
year = "2018",
month = aug,
doi = "10.1016/j.ssnmr.2018.03.003",
language = "English",
volume = "92",
pages = "7--11",
journal = "Solid State Nuclear Magnetic Resonance",
issn = "0926-2040",
publisher = "ACADEMIC PRESS INC ELSEVIER SCIENCE",

}

RIS

TY - JOUR

T1 - Two-dimensional 1H and 1H-detected NMR study of a heterogeneous biocatalyst using fast MAS at high magnetic fields

AU - Varghese, Sabu

AU - Halling, Peter J.

AU - Häussinger, Daniel

AU - Wimperis, Stephen

N1 - This is the author’s version of a work that was accepted for publication in Solid State Nuclear Magnetic Resonance. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Solid State Nuclear Magnetic Resonance, 92, 2018 DOI: 10.1016/j.ssnmr.2018.03.003

PY - 2018/8

Y1 - 2018/8

N2 - Abstract 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 1H and 1H-detected NMR experiments were performed with fast magic angle spinning (νR = 75 kHz) and at high magnetic fields (B0 = 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 1H-1H NOESY-type correlation experiments were able to provide information on 1H 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 1H-1H 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 1H-15N spectra of the immobilized enzyme and the solution-state enzyme confirmed that the structural integrity of the protein is well preserved upon covalent immobilization.

AB - Abstract 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 1H and 1H-detected NMR experiments were performed with fast magic angle spinning (νR = 75 kHz) and at high magnetic fields (B0 = 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 1H-1H NOESY-type correlation experiments were able to provide information on 1H 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 1H-1H 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 1H-15N spectra of the immobilized enzyme and the solution-state enzyme confirmed that the structural integrity of the protein is well preserved upon covalent immobilization.

KW - Immobilized enzymes

KW - Heterogeneous biocatalysts

KW - Solid-state NMR

KW - Biocatalysis

KW - 1H MAS NMR

KW - Epoxy-functionalized silica

KW - Human carbonic anhydrase II

KW - hCA II

KW - Covalent immobilization

U2 - 10.1016/j.ssnmr.2018.03.003

DO - 10.1016/j.ssnmr.2018.03.003

M3 - Journal article

VL - 92

SP - 7

EP - 11

JO - Solid State Nuclear Magnetic Resonance

JF - Solid State Nuclear Magnetic Resonance

SN - 0926-2040

ER -