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| - Measuring Protein Concentrations by NMR Spectroscopy
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| - In applications of NMR to biological macromolecules in solution, the concentration of the NMRsample is an important parameter describing the sample and providing information for the selection andplanning of experiments. Although concentrations can be measured directly by NMR spectroscopy, othermethods are usually preferred to measure the concentration of macromolecules in NMR samples. Thereasons are the difficulties in the correlation of the sample of interest with the signal intensity representinga known concentration. This correlation is usually obtained by adding to the sample a reference compoundwith known concentration and comparing the integral over resolved resonance lines of the molecules withknown and unknown concentrations. For solutions of biological macromolecules it is very difficult to find acompound that does not interact with the macromolecules and has a resonance outside their spectralrange. We introduce PULCON which is a method that correlates the absolute intensities of two spectrameasured in different solution conditions. PULCON is easy to implement and apply on all NMRspectrometers; it does not need any special hardware or software. PULCON is very robust and at thesame time delivers accurate concentrations of samples in the NMR tube. We demonstrate that PULCONhas the potential to replace UV spectroscopy for concentration measurements of NMR samples.
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