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NMR processing:
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Ab initio:
GeNMR
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Fragment-based:
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Template-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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NMR model quality:
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RDCs:
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Pseudocontact shifts:
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NMR spectrum prediction:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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Proshift
PPM
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From sequence:
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Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
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Solid-state NMR:
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Default Biocatalytic reductive amination as a route to isotopically labelled amino acids suitable for analysis of large proteins by NMR

Biocatalytic reductive amination as a route to isotopically labelled amino acids suitable for analysis of large proteins by NMR

We demonstrate an atom-efficient and easy to use H(2)-driven biocatalytic platform for the enantioselective incorporation of ˛H-atoms into amino acids. By combining the biocatalytic deuteration catalyst with amino acid dehydrogenase enzymes capable of reductive amination, we synthesised a library of multiply isotopically labelled amino acids from low-cost isotopic precursors, such as ˛H(2)O and ^(15)NH(4)^(+). The chosen approach avoids the use of pre-labeled ˛H-reducing agents, and therefore...

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