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NMR processing:
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PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
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ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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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:
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:
UPLABEL
Solid-state NMR:
sedNMR


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Old 09-29-2012, 11:56 AM
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Default Silk Structure studied with Nuclear Magnetic Resonance

Silk Structure studied with Nuclear Magnetic Resonance


Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy

Tetsuo Asakura, Yu Suzuki, Yasumoto Nakazawa, Koji Yazawa, Gregory P. Holland, Jeffery L. Yarger








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