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10.1007/s12551-017-0337-8 http://scihub22266oqcxt.onion/10.1007/s12551-017-0337-8 C5899698!5899698!29168118     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Rev 2018 ; 10 (2): 235-9 Nephropedia Template TP {{tp|p=29168118|t=2018. Ion?protein interactions of a potassium ion channel studied by attenuated total reflection Fourier transform infrared spectroscopy |pdf=|usr=}}{{29168118}} gab.com Text Ion protein interactions of a potassium ion channel studied by attenuated total reflection Fourier transform infrared spectroscopy JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=29168118 #FOAvip An understanding of ion?protein interactions is key to a better understanding of the molecular mechanisms of proteins, such as enzymes, ion channels, and ion pumps. A potassium ion channel, KcsA, has been extensively studied in terms of ion selectivity. Alkali metal cations in the selectivity filter were visualized by X-ray crystallography. Infrared spectroscopy has an intrinsically higher structural sensitivity due to frequency changes in molecular vibrations interacting with different ions. In this review article, I attempt to summarize ion-exchange-induced differences in Fourier transform infrared spectroscopy, as applied to KcsA, to explain how this method can be utilized to study ion?protein interactions in the KcsA selectivity filter. A band at 1680 cm?1 in the amide I region would be a marker band for the ion occupancy of K+, Rb+, and Cs+ in the filter. The band at 1627 cm?1 observed in both Na+ and Li+ conditions suggests that the selectivity filter similarly interacts with these ions. In addition to the structural information, the results show that the titration of K+ ions provides quantitative information on the ion affinity of the selectivity filter. Twit Text FOAVip Ion protein interactions of a potassium ion channel studied by attenuated total reflection Fourier transform infrared spectroscopy ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=29168118 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29168118 #FOAvip English Wikipedia <ref>{{Cite pmid|29168118}}</ref> Ion?protein interactions of a potassium ion channel studied by attenuated total reflection Fourier transform infrared spectroscopy #MMPMID29168118 Furutani Y Biophys Rev 2018[Apr]; 10 (2): 235-9 PMID29168118show ga An understanding of ion?protein interactions is key to a better understanding of the molecular mechanisms of proteins, such as enzymes, ion channels, and ion pumps. A potassium ion channel, KcsA, has been extensively studied in terms of ion selectivity. Alkali metal cations in the selectivity filter were visualized by X-ray crystallography. Infrared spectroscopy has an intrinsically higher structural sensitivity due to frequency changes in molecular vibrations interacting with different ions. In this review article, I attempt to summarize ion-exchange-induced differences in Fourier transform infrared spectroscopy, as applied to KcsA, to explain how this method can be utilized to study ion?protein interactions in the KcsA selectivity filter. A band at 1680 cm?1 in the amide I region would be a marker band for the ion occupancy of K+, Rb+, and Cs+ in the filter. The band at 1627 cm?1 observed in both Na+ and Li+ conditions suggests that the selectivity filter similarly interacts with these ions. In addition to the structural information, the results show that the titration of K+ ions provides quantitative information on the ion affinity of the selectivity filter. äIon?protein interactions of a potassium ion channel studied by attenua(epmc).pdf DeepDyve Pubget Overpricing