Biothermodynamics, Part 1 by Michael L. Johnson, Jo M. Holt, Gary K. Ackers

By Michael L. Johnson, Jo M. Holt, Gary K. Ackers

Within the final numerous years there was an explosion within the skill of biologists, molecular biologists and biochemists to gather huge quantities of information on their platforms. This quantity offers subtle equipment for estimating the thermodynamic parameters of particular protein-protein, protein-DNA and small molecule interactions.

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73 M using Eq. 14. Similar calculations are used to determine the final protein concentration as well. To measure refolding kinetics, one should prepare two stock protein samples (unfolded and native protein) and various urea-containing buffers that encompass the refolding transition. 5 M increments, and we average %20 injections per urea step. This requires 10 mL of urea-containing buffer for each final urea concentration and 15 mL of protein stock. 5 shows the procedure for preparing urea-containing buffer solutions as well as the final urea concentration calculated using Eq.

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Once the unfolded control sample is completed, remove the 8 M ureacontaining buffer. 5 M urea. One should note that whenever the solution conditions are drastically changed, one should rinse the syringe either with distilled, deionized water or with buffer to remove any remaining solution in the syringe. 7. Flush the system and acquire data as in step 5. 8. Continue to change the urea-containing buffer in the large drive syringe and acquire data by repeating steps 5–7 until the final buffer (0 M urea) is reached.

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