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PINE
Side-chains:
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Ab initio:
GeNMR
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UNIO ATNOS-Candid
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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:
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WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-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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iCing
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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:
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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:
sedNMR


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Old 11-19-2016, 08:35 PM
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Default Thermodynamic Additivity for Impacts of Base-PairSubstitutions on Association of the Egr-1 Zinc-Finger Proteinwith DNA

Thermodynamic Additivity for Impacts of Base-PairSubstitutions on Association of the Egr-1 Zinc-Finger Proteinwith DNA



Biochemistry
DOI: 10.1021/acs.biochem.6b00757



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