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Altogether, the high pressure NMR experiment has revealed a variety of fluctuating conformers of β-lactoglobulin, notably N, N′, I1, I2 and the totally unfolded conformer U. Fluctuation of N to I1 and I2 conformers with open barrel structures could be a common design of lipocalin family proteins which bind various hydrophobic compounds in its barrel structure.
Results are here presented in unfolded fraction units which are calculated from each spectra assuming than at time zero the elipticity recorded corresponds to the fully folded protein while at 200 h this parameter agrees with a totally unfolded state.
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