Selected Reaction Monitoring Mass Spectrometry (SRM-MS) in Proteomics

A Comprehensive View

Covering a wide-ranging facet of a "gold-standard" targeted mass spectrometry (MS) method for the consistent detection and accurate quantification of preselected proteins in complex biological matrices, Selected Reaction Monitoring Mass Spectrometry (SRM-MS) in Proteomics: A Comprehensive View describes:




The knowledge-based development of highly efficient SRM methodology including assay workflow, selection of proteins, peptides, transitions and its validation, and quality assessment
Available bioinformatic tools - for both pre-acquisition method development and post-MS acquisition data analysis and data repositories
Various relative and absolute quantification techniques
SRM-MS' widespread applications in biomarker development and in clinical studies, as well as in the analysis of various posttranslational modifications (PTMs)
Current challenges and contemporary trends to overcome those difficulties

In addition, it features the historical development of modern-day mass spectrometry with its vivid applications and also covers basic MS instrumentation, ionization techniques, and various proteomics approaches. Les mer
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Leveringstid: Sendes innen 21 dager
På grunn av Brexit-tilpasninger og tiltak for å begrense covid-19 kan det dessverre oppstå forsinket levering.

Om boka

Covering a wide-ranging facet of a "gold-standard" targeted mass spectrometry (MS) method for the consistent detection and accurate quantification of preselected proteins in complex biological matrices, Selected Reaction Monitoring Mass Spectrometry (SRM-MS) in Proteomics: A Comprehensive View describes:




The knowledge-based development of highly efficient SRM methodology including assay workflow, selection of proteins, peptides, transitions and its validation, and quality assessment
Available bioinformatic tools - for both pre-acquisition method development and post-MS acquisition data analysis and data repositories
Various relative and absolute quantification techniques
SRM-MS' widespread applications in biomarker development and in clinical studies, as well as in the analysis of various posttranslational modifications (PTMs)
Current challenges and contemporary trends to overcome those difficulties

In addition, it features the historical development of modern-day mass spectrometry with its vivid applications and also covers basic MS instrumentation, ionization techniques, and various proteomics approaches.

Comprehensive discussion, extensive references at the end of each chapter, and the list of review articles in the bibliography offer invaluable resources for advanced readings. Researchers from the undergraduate to postgraduate level and beyond in both academic or industry settings studying and working on mass spectrometry and/or proteomics will benefit from this book.

Fakta

Innholdsfortegnelse

Chapter 1: Introduction.- Chapter 2: The mass spectrometer and its components.- Chapter 3: Selected reaction monitoring mass spectrometry (SRM-MS).- Chapter 4: Development of SRM-MS experiment.- Chapter 5: Bioinformatics tools for SRM-MS.- Chapter 6: Quantification by SRM-MS.- Chapter 7: SRM-MS applications in proteomics.- Chapter 8: SRM-MS for posttranslational modification (PTM) analysis.- Chapter 9: Challenges, current trends and future directions.- Bibliography.- Index.

Om forfatteren

Mahmud Hossain, PhD, has extensive research experience on mass spectrometry-based proteomics in academia (Cornell University, New York with Professor Fred W. McLafferty), National Laboratory (Pacific Northwest National Laboratory, Washington with Dr. Richard D. Smith) and pharmaceutical industries (Merck Research Laboratories, and Sanofi, Massachusetts). He is a member of the American Society for Mass Spectrometry and co-authored several research papers in peer-reviewed journals and book chapters, and in numerous conference proceedings. His current research at Sanofi Genzyme includes drug discovery and development using shotgun/targeted proteomics and bioanalytics. He received his PhD in Bioanalytical Chemistry from University of Cincinnati, Ohio, under the guidance of Professor Patrick A. Limbach.