Solution structure of Syrian hamster prion protein rPrP(90-231). (Q30573700)

25 June 2017

title

Solution structure of Syrian hamster prion protein rPrP(90-231). (English)

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25 June 2017

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Prusiner SB

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25 June 2017

Cohen FE

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25 June 2017

Liu H

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25 June 2017

Farr-Jones S

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25 June 2017

Ulyanov NB

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25 June 2017

Llinas M

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25 June 2017

Marqusee S

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25 June 2017

Groth D

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25 June 2017

James TL

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25 June 2017

language of work or name

English

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publication date

1 April 1999

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25 June 2017

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25 June 2017

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25 June 2017

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25 June 2017

page(s)

5362-5377

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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

25 June 2017

cites work

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Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR

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NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231)

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A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform 1 1Edited by M. Yaniv

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Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods

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Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin

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Polypeptide chain folding in the hydrophobic core of hamster scrapie prion: analysis by X-ray diffraction

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A Gradient 13C NOESY-HSQC Experiment for Recording NOESY Spectra of 13C-Labeled Proteins Dissolved in H2O

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Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form.

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Chemical shifts as a tool for structure determination

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Identifiers

DOI

10.1021/BI982878X

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25 June 2017

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