• This topic has 2 replies, 3 voices, and was last updated 1 week, 4 days ago by Dominika Kowalczyk.
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    • March 3, 2026 at 21:20 #5865

      Hadar Amartely
      Participant

      Hi all
      Does anyone here use the Nanotemper Tycho NT 6 to measure thermal denaturation of proteins and can recommend or share his/her opinion about this instrument?
      Thanks!
      Hadar

    • March 4, 2026 at 09:19 #5868

      Cedric Montigny
      Participant

      Dear Hadar,
      We have used it a few times (available here on the PIM facility at I2BC, Gif sur Yvette, France ; https://www.i2bc.paris-saclay.fr/structural-biology/pim/). It is quick and easy to use. However, as the measurement highly dependents on the change in exposure of tryptophan residues to the solvent, the signal amplitude depends heavily on the number of tryptophan in the protein and, of course, on the protein concentration. Here, for a membrane transporter containing 11 tryptophan residues (MW=110 kDa), 10 of which being buried in the membrane (or in the detergent micelle), it is difficult to get nice signals below 1 mg/mL (but the sample is only a few microliters and you can easily repeat measurement to average data).
      Best
      Cédric

      • March 6, 2026 at 17:17 #5870

        Dominika Kowalczyk
        Participant

        Hi Hadar,
        I use it regularly at BioAscent and highly recommend it. I find it very useful to quickly compare buffers before running biophysical or biochemical assays, or to look how storage conditions affect protein stability. The signal will depend on the number of Trps in the sequence, like with any method that relies on intrinsic fluorescence, but overall, the sample consumption is small and you get the result in 3 min. It has its limitations but can be very useful 🙂
        Best,
        Dominika

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