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$destY = ($destHeight - $srcHeight) / 2; $white = imagecolorexact( $myCopyright, 255, 255, 255 ); imagecolortransparent( $myCopyright, $white ); imagecopy( $myImage, $myCopyright, $destX, $destY, 0, 0, $src width, $srcHeight ); in Figure 6.3 and one of the interesting observations we can make from such experiments is that, regardless of the denaturation treatment employed, most small proteins appear to denature completely over a remarkably narrow range of temperature, pH or denaturant concentration. This suggests that protein unfolding is a rapid and highly cooperative process. Spectroscopic techniques such as absorbance, uorescence and circular dichroism can be used to monitor folding/unfolding and to calculate the fraction of protein present in the U state at any particular temperature/pH/denaturant concentration. This fraction will be 0 when the protein is fully folded, 0.5 when 50% denatured and 1 when fully denatured. An equilibrium constant for 6.2 can be calculated from such measurements since K = [N ] [U ] (6.3)
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