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 titanic quantities of information on their structures. This quantity offers subtle equipment for estimating the thermodynamic parameters of particular protein-protein, protein-DNA and small molecule interactions.
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Additional resources for Biothermodynamics, Part 1
Angiogenesis: In Vitro Systems Edited by DAVID A. CHERESH VOLUME 444. Angiogenesis: In Vivo Systems (Part A) Edited by DAVID A. CHERESH VOLUME 445. Angiogenesis: In Vivo Systems (Part B) Edited by DAVID A. CHERESH VOLUME 446. Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death (Part B) Edited by ROYA KHOSRAVI-FAR, ZAHRA ZAKERI, RICHARD A. LOCKSHIN, AND MAURO PIACENTINI VOLUME 447. RNA Turnover in Bacteria, Archaea and Organelles Edited by LYNNE E. MAQUAT AND CECILIA M.
20 Jad Walters et al. DG ¼ DGH2 O À m½denaturant ð1:11Þ In this case, DGH2 O represents the free energy change in the absence of denaturant, and m represents the cooperativity index associated with the reaction. , 1995). For the two-state monomer described by Eq. 3). As a result, the apparent fraction of unfolded species is shown by Eq. 12. In this case, Y represents the signal obtained at each urea concentration. fapp ¼ ðYN À Y Þ K ¼ ðYN À YU Þ 1 þ K ð1:12Þ Taking into account Eqs. 12 and solving for Y, one can derive Eq.
The former provides information on the environmental changes of both tryptophan and tyrosine side chains due to the absorption wavelengths of both amino acids (280 nm and 275 nm, respectively). The latter provides a method to follow tryptophan emission selectively because there is little absorbance of tyrosines at 295 nm (Lackowicz, 2006). In general, there are two methods for collecting equilibrium unfolding data using fluorescence emission. In the first, one will obtain an emission spectrum for the native and unfolded samples (described subsequently).