A Calibration Routine for Efficient ETD in Large-Scale Proteomics

被引：42
作者：
Rose, Christopher M. [1 ,3 ]
Rush, Matthew J. P. [1 ,3 ]
Riley, Nicholas M. [1 ,3 ]
Merrill, Anna E. [1 ,3 ]
Kwiecien, Nicholas W. [1 ,3 ]
Holden, Dustin D. [4 ]
Mullen, Christopher [4 ]
Westphall, Michael S. [3 ]
Coon, Joshua J. [1 ,2 ,3 ]
机构：
[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA
[2] Univ Wisconsin, Dept Biomol Chem, Madison, WI 53706 USA
[3] Univ Wisconsin, Genome Ctr Wisconsin, Madison, WI 53706 USA
[4] Thermo Fisher Sci, San Jose, CA USA
来源：
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY | 2015年 / 26卷 / 11期
关键词：
ETD; Ion/ion; Kinetics; Proteomics; Mass spectrometry; Calibration; Orbitrap; ELECTRON-TRANSFER DISSOCIATION; QUADRUPOLE ION-TRAP; TRANSFER ION/ION REACTIONS; PROTEIN-SEQUENCE ANALYSIS; MASS-SPECTROMETRY; PEPTIDE IDENTIFICATION; MONOCLONAL-ANTIBODIES; SEARCH ALGORITHM; DOWN ANALYSIS; PROTON;
D O I：
10.1007/s13361-015-1183-1
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Electron transfer dissociation (ETD) has been broadly adopted and is now available on a variety of commercial mass spectrometers. Unlike collisional activation techniques, optimal performance of ETD requires considerable user knowledge and input. ETD reaction duration is one key parameter that can greatly influence spectral quality and overall experiment outcome. We describe a calibration routine that determines the correct number of reagent anions necessary to reach a defined ETD reaction rate. Implementation of this automated calibration routine on two hybrid Orbitrap platforms illustrate considerable advantages, namely, increased product ion yield with concomitant reduction in scan rates netting up to 75% more unique peptide identifications in a shotgun experiment.
引用
收藏
页码：1848 / 1857
页数：10
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