NMR spectroscopy can characterize proteins encapsulated in a sol-gel matrix

Korin E. Wheeler, Judith M. Nocek, Brian M Hoffman*

*Corresponding author for this work

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Proteins encapsulated within sol-gel matrices (SG) have the potential to fill many scientific and technological roles, but these applications are hindered by the limited means of probing possible structural consequences of encapsulation. We here present the first demonstration that it is possible to obtain high-resolution, solution NMR measurements of proteins encapsulated within a SG matrix. With the aim of determining the breadth of this approach, we have encapsulated three paramagnetic proteins with different overall charges: the highly acidic human Fe3+ cytochrome b5 (cyt b5); the highly basic horse heart cytochrome c (cyt c); and the nearly neutral, sperm whale cyanomet-myoglobin. The encapsulated anionic and neutral proteins (cyt b5; myoglobin) undergo essentially free rotation, but show minor conformational perturbations as revealed by shifts of contact-shifted peaks associated with the heme and nearby amino acids.

Original languageEnglish (US)
Pages (from-to)14782-14783
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number46
DOIs
StatePublished - Nov 22 2006

ASJC Scopus subject areas

  • Chemistry(all)

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