protein folding
Kenneth D. Hapner (khapner@montana.edu)
Wed, 16 Jun 1999 13:45:32 -0600
Dear Colleagues: We have expressed a 13kDa mammalian protein fragment from
bacteria. It was purified from inclusion bodies using a urea nickle column
procedure. After dialysis to remove the urea and dilution into "refolding
buffer", the protein is soluble below pH ~6.5 (pI is 8.9) but is unfolded
according to the NMR spectrum. What we need are some references or
unpublished "tricks" that others perhaps use to encourage the protein to
adopt a nonrandom and hopefully native conformation upon purification. If
you can offer some hints, we would be pleased to receive them. Thanks Ken
Hapner, Montana State University, khapner@montana.edu
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Kenneth D. Hapner
Department of Chemistry and Biochemistry
Montana State University
Bozeman, MT 59717-0310
khapner@gemini.oscs.montana.edu