FOURIER-TRANSFORM INFRARED SPECTROSCOPIC STUDIES ON THE EFFECT OF CYCLIC ADENOSINE-MONOPHOSPHATE ON THE SECONDARY STRUCTURE OF HUMAN ERYTHROCYTE-MEMBRANE PROTEINS

In this paper, the study on the effect of cAMP on erythrocyte membrane proteins by FTIR, deconvolution and curvefitting was reported. It was found that cAMP affects the secondary structure of membrane proteins by changing random and p-turn regions to the a-helix segments. The reg ulation of cAMP has a best concentration region, during which cAMP has the strongest regulating function. Meanwhile, cGMP and ATP has a nega tive effect on membrane proteins' secondary structure comparing to cAM P.