Unusual structural characteristics of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA

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 - 2010

Fingerprint

Circular dichroism spectroscopy
Oligomers
Dimers
Fluorescence
Proteins
Drug Discovery

Keywords

  • drug resistance
  • protein stability
  • Protein structure

ASJC Scopus subject areas

  • Spectroscopy

Cite this

Unusual structural characteristics of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA. / Khrapunov, S.; Cheng, H.; Hegde, Subray; Blanchard, John S.; Brenowitz, Michael D.

In: Spectroscopy, Vol. 24, No. 3-4, 2010, p. 339-341.

Research output: Contribution to journalArticle

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