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Ab initio:
GeNMR
Cyana
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Fragment-based:
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Refinement:
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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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From sequence:
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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
Camfold
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Isotope labeling:
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Solid-state NMR:
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Default 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.

1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.

Related Articles 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.

Biochemistry. 1992 Sep 22;31(37):8906-15

Authors: Okon M, Bray P, VuceliÄ? D

Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a single disulfide linkage. No evidence for any regular helical structure is found. Amide proton-solvent-exchange rate constants and 3JHN alpha coupling constants are evaluated.

PMID: 1390678 [PubMed - indexed for MEDLINE]



Source: PubMed
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