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 gigantic quantities of knowledge on their platforms. This quantity offers refined equipment for estimating the thermodynamic parameters of particular protein-protein, protein-DNA and small molecule interactions.
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Extra info for Biothermodynamics, Part 1
2B–C). If the first step is protein concentration dependent (Eq. 5, Fig. 2B), then the dimer dissociates in the first transition to yield a monomeric intermediate. In contrast, protein concentration dependence in the second transition indicates that subunit dissociation occurs after formation of a dimeric intermediate (Eq. 6, Fig. 2C). 4, one should note that similar models exist for heterodimers, depending on how the subunits of the heterodimer are treated. , 2005), for example, the subunits were assumed to be identical.
Add the urea into the beaker and record the weight. 4. 6 g. Record the weight. 5. Cover the beaker and stir until the urea dissolves. One should expect this to take 3 to 4 h. 1 (A) Emission spectra following excitation at 280 nm. Data for 0 M (○) and 8 M (□) urea are shown. In this example, the dotted line indicates a wavelength at which unfolding may be monitored due to a large difference in signal between the native and unfolded protein. (B) Equilibrium unfolding curve monitored by fluorescence emission at 320 nm (excitation at 280 nm).
8 Jad Walters et al. 6. When dissolved, check the pH using a recently calibrated pH meter. 5, accordingly. 7. Filter before use. Once the urea stock is prepared, the molarity is determined based on the recorded weights from steps 3 and 4 and from the refractive index, as described by Pace (1986). If the difference in the calculated molarity from each method is less than 10%, then the urea may be used. If it is greater than 10%, then the urea must be prepared again. Upon completion, the urea may be stored at À80 C until used.