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Ab initio:
GeNMR
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Fragment-based:
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Structure from chemical shifts:
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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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From structure:
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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:
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Protein solubility:
camLILA
ccSOL
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camGroEL
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Isotope labeling:
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Solid-state NMR:
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Old 12-15-2023, 05:49 AM
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Default Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure

Characterization of the zinc finger ?-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure

It is increasingly recognized that very small proteins (?-proteins) are ubiquitously found in all species of the three domains of life, and that they fulfill important functions. The halophilic archaeon Haloferax volcanii contains 282 ?-proteins of less than 70 amino acids. Notably, 43 of these contain two C(P)XCG motifs, suggesting their potential to complex a zinc ion. To explore the significance of these proteins, 16 genes encoding C(P)XCG proteins had been deleted, and the majority of...

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