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Template-based:
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Refinement:
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Structure from chemical shifts:
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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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Chemical shifts re-referencing:
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NMR model quality:
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Flexibility from structure:
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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:
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Isotope labeling:
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Solid-state NMR:
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Default Selective NMR Experiments on Macromolecules: Implementation and Analysis of QUIET-NOE

Selective NMR Experiments on Macromolecules: Implementation and Analysis of QUIET-NOESY.

Related Articles Selective NMR Experiments on Macromolecules: Implementation and Analysis of QUIET-NOESY.

J Magn Reson. 1998 Jun;132(2):204-13

Authors: Esposito G, Viglino P, Fogolari F, Gaestel M, Carver JA

The QUIET-NOESY experiment (Zwahlen et al., J. Am. Chem Soc. 116, 362-368, 1994) is applied to measure the mobility of the flexible extensions in the large aggregate (800 kDa) of a small heat-shock protein. The proper choices of the experimental protocol and parameters are discussed in order to employ a simplified data analysis procedure. Further experimental verification of the proposed strategy is also presented using the cyclic peptide gramicidin S as a model compound. Under suitable conditions, the determinations based on the analysis of QUIET-NOESY data are affected to a negligible extent by the approximations that are introduced by the proposed approach. Copyright 1998 Academic Press.

PMID: 9632546 [PubMed - as supplied by publisher]



Source: PubMed
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