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New Reagents for ESI 'Supercharging' of Noncovalent Protein Complexes and Denatured Proteins

机译:非价蛋白复合物的ESI“增压”的新试剂和变性蛋白质

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Few studies have reported effective means to increase ESI-charging beyond that measured under normal experimental conditions. Increasing the charge carried by analytes is desirable, because higher charged molecules are more effectively dissociated by tandem MS and because they reduce analyzer m/z requirements. Recently, we demonstrated that multiple charging of native proteins and noncovalent protein complexes could be increased in ESI-MS when spectra are obtained from no denaturing protein solutions containing up to 1percent (v/v) mnitrobenzyl alcohol (m-NBA). (Lomeli et al, JASMS 2009) Charge increased by +8percent to +48percent for the native proteins measured. Now we present other compounds as potent as m-NBA for supercharging under both native and denaturing conditions, and discuss possible physical and chemical properties impacting multiple charging behavior.
机译:少数研究报告了有效手段,以在正常实验条件下测量的eSI充电增加。期望增加分析物携带的电荷,因为通过串联MS更有效地解离电荷分子,因为它们降低了分析仪M / Z要求。最近,我们证明,当从含有高达1(v / v)酰硝基醇(M-NBA)的蛋白质溶液获得的光谱,在ESI-MS中可以增加天然蛋白质和非共价蛋白质复合物的多重充电。 (Lomeli等,JASMS 2009)电荷增加+ 8%+ 48%,用于测量的天然蛋白质。现在我们将其他化合物呈现为在天然和变性条件下的高增压的M-NBA的效率,并讨论可能的物理和化学性质,影响多种充电行为。

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