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NMR processing:
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Side-chains:
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NOEs:
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Ab initio:
GeNMR
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
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Secondary structure from chemical shifts:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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PPM
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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
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NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
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Default DNP NMR spectroscopy reveals new structures, residues and interactions in wild spider silks.

DNP NMR spectroscopy reveals new structures, residues and interactions in wild spider silks.

Related Articles DNP NMR spectroscopy reveals new structures, residues and interactions in wild spider silks.

Chem Commun (Camb). 2019 Apr 16;55(32):4687-4690

Authors: Craig HC, Blamires SJ, Sani MA, Kasumovic MM, Rawal A, Hook JM

Abstract
DNP solid state NMR spectroscopy allows non-targeted analysis of wild spider silk in unprecedented detail at natural abundance, revealing hitherto unreported features across several species. A >50-fold signal enhancement for each silk, enables the detection of novel H-bonding networks and arginine conformations, and the post-translational modified amino acid, hydroxyproline.


PMID: 30938741 [PubMed - indexed for MEDLINE]



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