Surface-mediated unfolding

The surface-mediated unfolding of proteins as measured by LC can be better visualized in Figure 4. The three major plasma proteins were chromatographed using various gradients to accelerate or delay their time of desorption. The longer their desorption was delayed (at 37 C), the greater the loss, or the smaller the amount... 

In addition, it was also shown [44] that DTAB-mediated elutabihty was positively eorrelated with the thermal struetural stability of the above-mentioned types of lysozyme. In other words, the resistance to elutabihty eorrelates with 02/0 ratio, the nonremovable fractional surface eoverage divided by the removable fractional siuface coverage, which, in turn, correlates with the extent of surface-indueed unfolding (i.e., in our case). As far as the surface-induced unfolding on the hydrophihe surface is eoneemed, the least thermally stable mutant (i.e., BW) exhibited the highest value of f/gju, whereas the wild type exhibited the lowest value of Apparently, there is a switch in order between the wild type and the most stable form, which is DC. It was shown [19] that the speetral differenees between the wild type and I3C were relatively small. Nevertheless, the differenee in kinetie behavior between the wild type and I3C is small, compared with that of I3W. 

It is clear that the transition from one chevron to the other cannot take place abruptly in a layer as sketched in (d), as this would lead to a surface (2D) defect with no continuity of layer structure nor director field. Instead it is mediated by an unfolded part of width w (this region will be observed as a wall of thickness w) in (e), looked at from the top as when observing the sample... 

---