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Ab initio:
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
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Default Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study [Biochemistry]

Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study [Biochemistry]

Gaston Courtade, Luisa Ciano, Alessandro Paradisi, Peter J. Lindley, Zarah Forsberg, Morten Sorlie, Reinhard Wimmer, Gideon J. Davies, Vincent G. H. Eiȷsink, Paul H. Walton, Finn L. Aachmann...
Date: 2020-08-11

Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to activate molecular oxygen for subsequent oxidative cleavage of glycosidic bonds. To provide insight into the mode of action of these industrially important enzymes, we have performed an integrated NMR/electron paramagnetic resonance (EPR) study into the detailed aspects of an AA10 LPMO–substrate... Read More


PNAS:
Number: 32
Volume: 117
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