One of the major obstacles facing the field of structural biology in the post genomic era is the inherent difficulty of analyzing the structure of membrane proteins under native conditions. The method of choice for st...One of the major obstacles facing the field of structural biology in the post genomic era is the inherent difficulty of analyzing the structure of membrane proteins under native conditions. The method of choice for studying such proteins is FTIR spectroscopy. Following the outbreaking of the severe acute respiratory syndrome （SARS） virus, in 2003, extensive work has been directed at elucidating the structure of the E transmembrane proteins of the SARS coronavirus. In this study, the secondary structure of the transmembrane a-helical bundles was analysised using the biophysical method site specific infrared dichroism （SSID）. Sixteen amino acids were isotopically labeled with （~3C=180） at different positions of the primary structure of the synthesized E protein CoV. The secondary structure was studied using Attenuated Total Internal Reflection （ATR） FTIR spectroscopy. Based on our findings, the presence of two possible H-bonding interactions between the carbonyl oxygen of two residues 26 and 31 （Phe and Leu） respectively with water molecules which may be trapped within the helix structure were postulatesed. These interactions may cause a change in this structure.展开更多
文摘One of the major obstacles facing the field of structural biology in the post genomic era is the inherent difficulty of analyzing the structure of membrane proteins under native conditions. The method of choice for studying such proteins is FTIR spectroscopy. Following the outbreaking of the severe acute respiratory syndrome （SARS） virus, in 2003, extensive work has been directed at elucidating the structure of the E transmembrane proteins of the SARS coronavirus. In this study, the secondary structure of the transmembrane a-helical bundles was analysised using the biophysical method site specific infrared dichroism （SSID）. Sixteen amino acids were isotopically labeled with （~3C=180） at different positions of the primary structure of the synthesized E protein CoV. The secondary structure was studied using Attenuated Total Internal Reflection （ATR） FTIR spectroscopy. Based on our findings, the presence of two possible H-bonding interactions between the carbonyl oxygen of two residues 26 and 31 （Phe and Leu） respectively with water molecules which may be trapped within the helix structure were postulatesed. These interactions may cause a change in this structure.
