Abstract
Protein folding/unfolding processes involve a large number of weak, non-covalent interactions and are more appropriately described in terms of the movement of a point representing protein conformation in a plot of internal free energy versus conformational degrees of freedom. While these energy landscapes have an astronomically large number of dimensions, it has been shown that many relevant aspects of protein folding can be understood in terms of their projections onto a few relevant coordinates. Remarkably, such low-dimensional free energy surfaces can be obtained from experimental DSC data using suitable analytical models. Here, we describe the experimental procedures to be used to obtain the high-quality DSC data that are required for free-energy surface analysis.
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