The Fas TMD was reconstituted in q = 0.7 bicelles and DHPC was progressively added to reduce the bicelle size. The detergent was taken from a concentrated stock solution (660 mM DHPC) made in the same buffer of the protein sample and it was added in small aliquots (few μL per step) to minimize possible dilution effects. To monitor the progress of the titration by NMR, a 2D 1H-15N TROSY-HSQC spectrum was recorded at 600 MHz (Table S1 ) at each of the following q values: 0.7, 0.6, 0.5, 0.4 and 0.3. The chemical shift assignments of the human Fas TMD was taken from the Biological Magnetic Resonance Bank (BMRB)[20 (link)], entry 25930[1c (link)].
Protocol detail
Titration of Fas Transmembrane Domain
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Corresponding Organization : Harvard University
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Variable analysis
independent variables
- Q (bicelle size)
- Chemical shift changes in 2D 1H-15N TROSY-HSQC spectrum
- Buffer composition
- Protein sample
- Experimental conditions (600 MHz NMR)
- No positive or negative controls were explicitly mentioned.
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