KCS

Human transmembrane proteins (hTMPs) perform essential role like gateway to permit the transport of specific substances. Additionally channel formation, cell-to-cell communication and signal transductions are also important tasks of hTMPs. The starting point for understanding and studying the specific biochemical processes of hTMPs is to determine their three-dimensional structure. The study of the structure of these membrane proteins has been extensively studied because it forms the foundation for new drugs development. The first is the transmembrane domain of amyloid precursor proteins (APP-TM) related Alzheimer’s disease. What we pay attention to is the formation of amyloid channels that cause side effects such as and abnormal increase in intracellular calcium concentration. In other words, APP-TM forms a Ca2+ permeable ion channel in the cell membrane, destroying calcium homeostasis in normal cells, and such amyloid channels are also found in other amyloidogenic disease-related proteins such as prions and α-synuclein. The next is Syndecan-4 (Syd4), which is involved in signal transduction and cancer progression. They may affect tissue development and repair and grow factors as well as the pathogenesis of numerous diseases, especially such as cancer. The main process of action mechanism of Syd4 is the signal transmission through structural changes by ligand binding, so it is important to examine the three-dimensional structure in order to understand this process. High-purity protein samples obtained from optimized expression and purification processes have been characterized using various analytical techniques and are undergoing structural studies using solution/ solid-state NMR spectroscopy and computer modeling.