By Stefanie Mädler, Elisabetta Boeri Erba (auth.), Zongwei Cai, Shuying Liu (eds.)
MALDI-ToF Mass Spectrometry for learning Noncovalent Complexes of Biomolecules, by means of Stefanie Mädler, Elisabetta Boeri Erba, Renato Zenobi program of MALDI-TOF-Mass Spectrometry to Proteome research utilizing Stain-Free Gel Electrophoresis, via Iuliana Susnea, Bogdan Bernevic, Michael Wicke, Li Ma, Shuying Liu, Karl Schellander, Michael Przybylski MALDI Mass Spectrometry for Nucleic Acid research, through Xiang Gao, Boon-Huan Tan, Richard J. Sugrue, Kai Tang decision of Peptide and Protein Disulfide Linkages by way of MALDI Mass Spectrometry, via Hongmei Yang, Ning Liu, Shuying Liu MALDI In-Source Decay, from Sequencing to Imaging, through Delphine Debois, Nicolas Smargiasso, Kevin Demeure, Daiki Asakawa, Tyler A. Zimmerman, Loïc Quinton, Edwin De Pauw Advances of MALDI-TOF MS within the research of conventional chinese language drugs, via Minghua Lu, Zongwei Cai Chemical and Biochemical purposes of MALDI TOF-MS in accordance with studying the Small natural Compounds, via Haoyang Wang, Zhixiong Zhao, Yinlong Guo Bioinformatic research of knowledge Generated from MALDI Mass Spectrometry for Biomarker Discovery, through Zengyou He, Robert Z. Qi, Weichuan Yu
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Additional resources for Applications of MALDI-TOF Spectroscopy
38 41 41 41 42 43 43 43 43 48 48 52 53 Abbreviations 1D 2D MALDI-TOF MS PMF SDS-PAGE One-dimensional gel electrophoresis Two-dimensional gel electrophoresis Matrix assisted laser desorption/ionization–time-of-flight Mass spectrometry Peptide mass fingerprinting Sodium dodecyl sulfate polyacrylamide gel electrophoresis 1 Introduction Matrix assisted laser desorption/ionization–mass spectrometry (MALDI-MS), introduced by Karas and Hillenkamp in 1988 [1, 2], is now widely used in proteomics studies.
Bahr U, Ayg€un H, Karas M (2008) Detection and relative quantification of siRNA double strands by MALDI mass spectrometry. Anal Chem 80:6280–6285 75. Sudha R, Zenobi R (2002) The detection and stability of DNA duplexes probed by MALDI mass spectrometry. Helv Chim Acta 85:3136–3143 76. Distler AM, Allison J (2002) Additives for the stabilization of double-stranded DNA in UVMALDI MS. J Am Soc Mass Spectrom 13:1129–1137 77. Luo SZ, Li YM, Qiang W et al (2004) Detection of specific noncovalent interaction of peptide with DNA by MALDI-TOF.
Methods . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1 Protein Separation by Gel Electrophoresis . . . . . . . . . . . . . . . . . . . . . . 2 Gel Bioanalyzer for Protein Detection and Visualization . . . . . . . . . . . . . . 3 In-Gel Proteolytic Digestion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4 MALDI-TOF-Mass Spectrometry . .