The unfolding of proteins during denaturation by guanidine or urea has been extensively studied. However, the methods hitherto employed usually provide only a limited amount of information on gross changes of such mol...The unfolding of proteins during denaturation by guanidine or urea has been extensively studied. However, the methods hitherto employed usually provide only a limited amount of information on gross changes of such molecular properties as shape, size, or the exposure of buried aromatic residues. CD studies are hampered by high absorption of the denaturants commonly employed in the far ultraviolet region. Recent development in Fourier展开更多
基金Project supported in part by the National Natural Science Foundation of China.
文摘The unfolding of proteins during denaturation by guanidine or urea has been extensively studied. However, the methods hitherto employed usually provide only a limited amount of information on gross changes of such molecular properties as shape, size, or the exposure of buried aromatic residues. CD studies are hampered by high absorption of the denaturants commonly employed in the far ultraviolet region. Recent development in Fourier
