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Article

Correlation of the sweetness of variants of the protein brazzein with patterns of hydrogen bonds detected by NMR spectroscopy.

The Journal of biological chemistry - 15 Aug 2003

Assadi-Porter Fariba M, Abildgaard Frits, Blad Heike, Markley John L

Abstract excerpt

In sequence-function investigations, approaches are needed for rapidly screening protein variants for possible changes in conformation. Recent NMR methods permit direct detection of hydrogen bonds through measurements of scalar couplings that traverse hydrogen bonds (trans-hydrogen bond couplings). We have applied this approach to screen a series of five single site mutants of the sweet protein brazzein with...

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Identifiers

PMID: 12732626
DOI: 10.1074/jbc.M302663200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Correlation of the sweetness of variants of the protein brazzein with patterns of hydrogen bonds detected by NMR spectroscopy.PMID 12732626Read ↗

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Brazzein a small, sweet protein: discovery and physiological overview.Semantic proximity Read ↗

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