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Biosilica‐Entrapped Enzymes Studied by Using Dynamic Nuclear‐Polarization‐Enhanced High‐Field NMR Spectroscopy
Author(s) -
Ravera Enrico,
Michaelis Vladimir K.,
Ong TaChung,
Keeler Eric G.,
Martelli Tommaso,
Fragai Marco,
Griffin Robert G.,
Luchinat Claudio
Publication year - 2015
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201500549
Subject(s) - magic angle spinning , chemistry , nuclear magnetic resonance spectroscopy , spectroscopy , reusability , combinatorial chemistry , materials science , chemical engineering , organic chemistry , computer science , physics , quantum mechanics , engineering , software , programming language
Enzymes are used as environmentally friendly catalysts in many industrial applications, and are frequently immobilized in a matrix to improve their chemical stability for long‐term storage and reusability. Recently, it was shown that an atomic‐level description of proteins immobilized in a biosilica matrix can be attained by examining their magic‐angle spinning (MAS) NMR spectra. However, even though MAS NMR is an excellent tool for determining structure, it is severely hampered by sensitivity. In this work we provide the proof of principle that NMR characterization of biosilica‐entrapped enzymes could be assisted by high‐field dynamic nuclear polarization (DNP).