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NMR processing:
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Ab initio:
GeNMR
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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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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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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RDCs:
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NMR spectrum prediction:
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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
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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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Default An efficient NMR approach for obtaining sequence-specific resonance assignments of la

An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.

Related Articles An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.

FEBS Lett. 1990 Jun 18;266(1-2):155-8

Authors: Ikura M, Krinks M, Torchia DA, Bax A

By simultaneously incorporating in a protein 13C-carbonyl- and 15N-labeled amino acids with different levels of enrichment, characteristics asymmetric doublet-like patterns are observed for 15N nuclei that are directly adjacent to the 13C1-labeled residues, providing unambiguous identification of a large number of unique dipeptide fragments of the protein. Additional assignments and qualitative structural information can be obtained from such a selectively labeled protein by recording multiple bond correlation spectra. The procedure is demonstrated for the protein calmodulin, complexed with calcium.

PMID: 2114317 [PubMed - indexed for MEDLINE]



Source: PubMed
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