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Data processing handbook for complex biological data sources /

"[This book] provides relevant and to the point content for those who need to understand the different types of biological data and the techniques to process and interpret them. The book includes feedback the editor received from students studying at both undergraduate and graduate levels, and...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Misra, Gauri (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: London : Academic Press, 2019.
Temas:
Acceso en línea:Texto completo
Tabla de Contenidos:
  • Front Cover; Data Processing Handbook for Complex Biological Data Sources; Copyright Page; Dedication; Contents; List of contributors; Foreword by Jeremy C. Smith; Foreword by M.R.N. Murthy; Foreword by Aatto Laaksonen; Preface; Acknowledgments; 1 Mass spectroscopy; 1.1 Introduction; 1.1.1 Principle; 1.1.2 Instrumentation; 1.1.3 Types of ionization techniques; 1.1.3.1 Electron ionization; 1.1.3.2 Chemical ionization; 1.1.3.3 Fast atom bombardment; 1.1.3.4 Matrix assisted laser desorption ionization; 1.1.3.5 Electrospray ionization; 1.1.3.6 Fragmentation; 1.1.4 Analyzers
  • 1.1.4.1 Time of flight1.1.4.2 Quadrupole; 1.1.4.3 Ion trap analyzer; 1.1.4.4 Fourier transform-ion cyclotron resistance; 1.1.4.5 Orbitrap analyzer; 1.1.4.6 Tandem mass spectrometer; 1.1.5 Detectors; 1.1.5.1 Faraday cup; 1.1.5.2 Electron multipliers; 1.1.5.3 Photomultipliers; 1.1.5.4 Microchannel plate; 1.1.6 Mass interpretation; 1.1.6.1 Types of peaks; 1.1.6.2 Fragmentation rules; 1.1.6.3 Peptide mass fingerprinting; 1.1.6.4 Peptide fragmentation fingerprinting; 1.1.6.5 De novo peptide sequencing; 1.2 Raw data; 1.2.1 NanoLC principle; 1.2.2 Gradient; 1.2.3 Orbitrap technology
  • 1.2.4 Data-dependent acquisition1.3 Data processing; 1.3.1 Trans-proteomic pipeline; 1.3.2 Installation; 1.3.3 Raw file conversion; 1.3.4 Search engine support; 1.3.5 PeptideProphet for corroboration; 1.3.6 Pep3D to view chromatogram; 1.3.7 iProphet for peptide-level corroboration; 1.3.8 XPRESS/ASAP ratio for peptide quantitation; 1.3.9 Protein prophet for protein interpretation and corroboration; 1.4 Protein quantification and identification; 1.4.1 Label-free quantification; 1.4.2 Functional annotation and enrichment analysis; 1.5 Applications of mass spectrometry
  • 1.5.1 Application in proteomics1.5.2 Application in metabolomics; 1.5.3 Application in environment analysis; 1.5.4 Application in pharmacy; 1.5.5 Application in forensic science; 1.5.6 Applications in medical research; 1.6 Conclusion; References; Further Reading; 2 Circular dichroism; 2.1 Introduction; 2.2 Principle; 2.3 Raw data analyses; 2.3.1 Case study 1: to study acid-induced transitions in a protein; 2.3.2 Case study 2: to study pH-induced transitions in a protein; 2.3.3 Case study 3: to study structural transitions in nucleic acids
  • 2.3.4 Case study 4: determination of Tm and other thermodynamic parameters2.4 Miscellaneous examples; 2.5 Conclusion; Acknowledgments; References; 3 Fluorescence spectroscopy; 3.1 Introduction; 3.2 Principle; 3.2.1 Instrumentation; 3.3 Intrinsic fluorescence; 3.3.1 Protein stability studies; 3.3.2 Protein interaction studies; 3.4 Extrinsic fluorescence; 3.5 Fluorescence polarization; 3.6 Fluorescence resonance energy transfer; 3.7 Conclusion; Acknowledgment; References; 4 High-throughput sequencing; 4.1 Introduction; 4.2 High-throughput sequencing raw data