Mass spectrometry for proteomics

被引:475
作者
Han, Xuemei [1 ]
Aslanian, Aaron [1 ,2 ]
Yates, John R., III [1 ]
机构
[1] Scripps Res Inst, Dept Physiol Chem, La Jolla, CA 92037 USA
[2] Salk Inst Biol Studies, Mol & Cell Biol Lab, La Jolla, CA 92037 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/j.cbpa.2008.07.024
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mass spectrometry has been widely used to analyze biological samples and has evolved into an indispensable tool for proteomics research. Our desire to understand the proteome has led to new technologies that push the boundary of mass spectrometry capabilities, which in return has allowed mass spectrometry to address an ever-increasing array of biological questions. The recent development of a novel mass spectrometer (Orbitrap) and new dissociation methods such as electron-transfer dissociation has made possible the exciting new areas of proteomic application. Although bottom-up proteomics (analysis of proteolytic peptide mixtures) remains the workhorse for proteomic analysis, middle-down and topdown strategies (analysis of longer peptides and intact proteins, respectively) should allow more complete characterization of protein isoforms and post-translational modifications. Finally, stable isotope labeling strategies have transformed mass spectrometry from merely descriptive to a tool for measuring dynamic changes in protein expression, interaction, and modification.
引用
收藏
页码:483 / 490
页数:8
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