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GeNMR
Cyana
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Fragment-based:
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Structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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Molecular dynamics:
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From structure:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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Isotope labeling:
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Solid-state NMR:
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Old 10-17-2024, 06:23 PM
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Default (19)F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH

(19)F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH

The recent application of ^(19)F NMR in the study of biomolecular structure and dynamics has made it a potentially attractive probe to complement traditional ^(15)N/^(13)C labelled probes for backbone and sidechain dynamics, albeit with some complications. The utility of ^(15)N relaxation rates of rigid backbone amide groups to determine the rotational diffusion tensor of proteins is well established. Here we show that the measured ^(19)F relaxation rates of two buried and possibly immobile...

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