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. Author manuscript; available in PMC: 2013 Feb 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Jul 22;1818(2):178–182. doi: 10.1016/j.bbamem.2011.07.019

Figure 1.

Figure 1

Thermodynamic cycle for partitioning-folding of an α-helical peptide in the membrane interface (modified from [7]). State A is the fully unfolded peptide in water; B is the fully unfolded peptide in the interface; C is the actual state of peptide in water, which is an ensemble of folded and unfolded conformations; and state D is the peptide in a α-helical conformation partitioned into the membrane interface. The conformation is not necessarily, and usually isn’t, fully α-helical. States A and B are virtual states that cannot be observed experimentally due to their low occupancy. The free-energy difference, ΔGAB, is computed using the experiment-based algorithm of Hristova and White [10]. The other free-energy differences are determined experimentally (Figure 2).