Ontology highlight
ABSTRACT:
SUBMITTER: Khrapunov S
PROVIDER: S-EPMC3166997 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Khrapunov Sergei S Brenowitz Michael M
Biophysical chemistry 20110505 1
MfpA from Mycobacterium tuberculosis is a founding member of the pentapeptide repeat class of proteins (PRP) that is believed to confer bacterial resistance to the drug fluoroquinolone by mimicking the size, shape and surface charge of duplex DNA. We show that phenylalanine side chain stacking stabilizes the N-terminus of MfpA's pentapeptide thus extending the DNA mimicry analogy. The Lumry-Eyring model was applied to multiple spectral measures of MfpA denaturation revealing that the MfpA dimer ...[more]