In general, proteins become functional once they fold into a specific globular structure. Moreover, this work provides a method for probing the individual temperature dependence of the different amino acid types, which is difficult to obtain by direct experiment. Alternatively, one can conclude that the temperature dependence of the hydrophobic effect has a measurable influence on protein structures. These propensities show that the hydrophobicity becomes weaker at lower temperatures, in line with current theory. Using NMR structures filtered for sequence identity, we were able to extract hydrophobicity propensities for all amino acids at five different temperature ranges (spanning 265-340 K). Here we investigate if it is possible to extract this temperature dependence directly from a large set of protein structures determined at different temperatures. This temperature dependence is thought to explain the denaturation of proteins at low temperatures. However, the hydrophobic force is known to be strongly temperature dependent. One can estimate the relative strength of this hydrophobic effect for each amino acid by mining a large set of experimentally determined protein structures. The hydrophobic effect is the main driving force in protein folding.
0 kommentar(er)
