These findings thus illustrate how the analysis of water-protein hydrogen bonds can reveal the molecular origins of protein behaviours associated with the hydrophobic effect.Ī detailed understanding of the molecular origins of the hydrophobic effect 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 in proteins and of its role as a driving force in protein folding and assembly 10, 11, 12, 13, 14 is still an open problem. Then, using Φ-value analysis we show that the structural differences between the hot and cold denatured states result in two alternative folding mechanisms. We thus find that the hot denatured state is more compact and richer in secondary structure than the cold denatured state, since water at lower temperatures can form more hydrogen bonds than at high temperatures. larger than 1 nm), because of the presence of complex surface patterns of polar and non-polar residues their behaviour can be compared to that of ‘small’ particles (i.e. Thus, even if proteins are ‘large’ particles (in terms of the hydrophobic effect, i.e. A detailed analysis of the resulting structures reveals that water molecules in the bulk and at the protein interface form on average the same number of hydrogen bonds. Towards this goal, we characterise the cold and hot denatured states of a protein by modelling NMR chemical shifts using restrained molecular dynamics simulations. A complete understanding of this effect requires the description of the conformational states of water and protein molecules at different temperatures.
The hydrophobic effect is a major driving force in protein folding.
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