Complete 1H and partial 13C resonance assignments at 37 and 22°C for brazzein, an intensely sweet protein

Jane E. Caldwell, Frits Abildgaard, Ding Ming, Göran Hellekant, John L. Markley

Research output: Contribution to journalArticlepeer-review

12 Scopus citations
Original languageEnglish (US)
Pages (from-to)231-232
Number of pages2
JournalJournal of biomolecular NMR
Volume11
Issue number2
DOIs
StatePublished - 1998

Bibliographical note

Funding Information:
This work was supported by a grant (GM35976) from the National Institute of General Medical Sciences, National Institutes of Health (NIH). NMR data were collected and processed at the National Magnetic Resonance Facility at Madison (NMRFAM) which is supported by a grant (RR02307) from the Biomedical Research Technology Program of the National Center for Research Resources, NIH. Equipment in NMRFAM was purchased with funds from the University of Wisconsin, the Biological Instrumentation Program of the National Science Foundation (grant DMB-8415048), the National Biomedical Research Technology Program (grant RR02301), the Shared Instrumentation Program of the NIH (grant RR02781), and the U.S. Department of Agriculture. One of us (J.C.) was supported in part by predoctoral fellowships from the National Science Foundation and the University of Wisconsin Alumni Research Foundation.

Keywords

  • Protein
  • Sweet
  • Thermostability

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