Folding of the ig-like domain of the dengue virus envelope protein analyzed by high-hydrostatic-pressure nmr at residue-level resolution

HIGHLIGHTS

  • who: Tomonori Saotome and collaborators from the Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Nakamachi, Koganei, Tokyo, Japan have published the Article: Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at Residue-Level Resolution, in the Journal: (JOURNAL)
  • how: In this study high-hydrostatic-pressure NMR was used to analyze at a residue-level resolution the folding pathway of DE4-ED3 an Ig-like protein domain from the dengue virus envelope.

SUMMARY

    The ED3 domain of . . .

     

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