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Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered
Magnus Kjærgaard, Flemming Martin Poulsen,
Kaare Teilum
Biomolecular Sciences
15
Citations (Scopus)
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Dive into the research topics of 'Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered'. Together they form a unique fingerprint.
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Keyphrases
Aliphatic Side Chain
20%
Chemical Shift
20%
Coactivator
100%
Conformational Selection
20%
Coupling Constant
20%
CREB-binding Protein
20%
Flexible Proteins
20%
Folded Proteins
20%
Free Protein
20%
Free State
20%
Highly Dynamic
100%
Hydrophobic Core
100%
Ligand-binding Domain
100%
Ligand-free
20%
Methyl
40%
Molecular Recognition
20%
Molten Globule
20%
NMR Techniques
20%
Order Parameter
20%
Overall Stability
20%
Protein Folding
20%
Protein Structure
20%
Retinoid X Receptor
20%
Side-chain Packing
20%
Structural Adjustment
20%
Structured Support
20%
Tertiary Structure
20%
Thyroid Hormone Receptor
20%
Titration
20%
Urea
20%
Well-defined Structure
20%
Well-ordered
100%
Biochemistry, Genetics and Molecular Biology
Molten Globule
20%
Retinoid Receptor
20%