Unusual structural characteristics of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA

S. Khrapunov, H. Cheng, S. Hegde, J. Blanchard, M. Brenowitz

Research output: Contribution to journalArticle

Abstract

The solution structure and refolding of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA was explored by fluorescence and circular dichroism spectroscopy. Our results show that MfpA exists in two stable structural forms which exclusively favor dimer or oligomer formation. The structural malleability of MfpA may provide a novel target for drug discovery.

Original languageEnglish (US)
Pages (from-to)339-341
Number of pages3
JournalSpectroscopy
Volume24
Issue number3-4
DOIs
StatePublished - Jul 26 2010

Keywords

  • Protein structure
  • drug resistance
  • protein stability

ASJC Scopus subject areas

  • Spectroscopy

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