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Side-chains:
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Ab initio:
GeNMR
Cyana
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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:
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Homology-based:
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Preditor
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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NMR spectrum prediction:
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Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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Proshift
PPM
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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
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Isotope labeling:
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Solid-state NMR:
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Old 11-18-2010, 09:15 PM
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Default Conformational changes in the human estrogen receptor observed by (19)F NMR.

Conformational changes in the human estrogen receptor observed by (19)F NMR.

Related Articles Conformational changes in the human estrogen receptor observed by (19)F NMR.

Biochem Biophys Res Commun. 2000 Apr 21;270(3):988-91

Authors: Luck LA, Barse JL, Luck AM, Peck CH

The (19)F NMR spectra of the 5F-Trp labeled glutathione-S-transferase fusion protein with residues 282-595 of the human estrogen receptor show that there is a distinct conformational change in the protein when estradiol is added to the unliganded protein. Our studies show the empty receptor to have more conformational flexibility than the liganded form. This study shows the applicability of (19)F NMR to study conformational change in large protein systems.

PMID: 10772938 [PubMed - indexed for MEDLINE]



Source: PubMed
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