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10.1007/s13361-016-1381-5 http://scihub22266oqcxt.onion/10.1007/s13361-016-1381-5 C4869745!4869745!27106602     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Am+Soc+Mass+Spectrom 2016 ; 27 (ä): 1099-104 Nephropedia Template TP {{tp|p=27106602|t=2016. Negative Ions Enhance Survival of Membrane Protein Complexes |pdf=|usr=}}{{27106602}} gab.com Text Negative Ions Enhance Survival of Membrane Protein Complexes JO: J Am Soc Mass Spectrom http://www.kidney.de/pget.php?&tw=1&pmid=27106602 #FOAvip Membrane protein complexes are commonly introduced to the mass spectrometer solubilized in detergent micelles. The collisional activation used to remove the detergent, however, often causes protein unfolding and dissociation. As in the case for soluble proteins, electrospray in the positive ion mode is most commonly used for the study of membrane proteins. Here we show several distinct advantages of employing the negative ion mode. Negative polarity can yield lower average charge states for membrane proteins solubilized in saccharide detergents, with enhanced peak resolution and reduced adduct formation. Most importantly, we demonstrate that negative ion mode electrospray ionization (ESI) minimizes subunit dissociation in the gas phase, allowing access to biologically relevant oligomeric states. Together, these properties mean that intact membrane protein ions can be generated in a greater range of solubilizing detergents. The formation of negative ions, therefore, greatly expands the possibilities of using mass spectrometry on this intractable class of protein.Graphical Abstract?Electronic supplementary material: The online version of this article (doi:10.1007/s13361-016-1381-5) contains supplementary material, which is available to authorized users. Twit Text FOAVip Negative Ions Enhance Survival of Membrane Protein Complexes ????J Am Soc Mass Spectrom http://www.kidney.de/pget.php?&tw=1&pmid=27106602 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27106602 #FOAvip English Wikipedia <ref>{{Cite pmid|27106602}}</ref> Negative Ions Enhance Survival of Membrane Protein Complexes #MMPMID27106602 Liko I; Hopper JTS; Allison TM; Benesch JLP; Robinson CV J Am Soc Mass Spectrom 2016[]; 27 (ä): 1099-104 PMID27106602show ga Membrane protein complexes are commonly introduced to the mass spectrometer solubilized in detergent micelles. The collisional activation used to remove the detergent, however, often causes protein unfolding and dissociation. As in the case for soluble proteins, electrospray in the positive ion mode is most commonly used for the study of membrane proteins. Here we show several distinct advantages of employing the negative ion mode. Negative polarity can yield lower average charge states for membrane proteins solubilized in saccharide detergents, with enhanced peak resolution and reduced adduct formation. Most importantly, we demonstrate that negative ion mode electrospray ionization (ESI) minimizes subunit dissociation in the gas phase, allowing access to biologically relevant oligomeric states. Together, these properties mean that intact membrane protein ions can be generated in a greater range of solubilizing detergents. The formation of negative ions, therefore, greatly expands the possibilities of using mass spectrometry on this intractable class of protein.Graphical Abstract?Electronic supplementary material: The online version of this article (doi:10.1007/s13361-016-1381-5) contains supplementary material, which is available to authorized users. äNegative Ions Enhance Survival of Membrane Protein Complexes (epmc).pdf DeepDyve Pubget Overpricing