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 language | English (US) |
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Pages (from-to) | 339-341 |
Number of pages | 3 |
Journal | Spectroscopy |
Volume | 24 |
Issue number | 3-4 |
DOIs | |
State | Published - 2010 |
Keywords
- Protein structure
- drug resistance
- protein stability
ASJC Scopus subject areas
- Spectroscopy