Biophysical Characterization of Proteins in Developing Biopharmaceuticals

Forfatter: info mangler
Bog
  • Format
  • Bog, paperback
  • Engelsk

Beskrivelse

Biophysical Characterization of Proteins in Developing Biopharmaceuticals, Second Edition, presents the latest on the analysis and characterization of the higher-order structure (HOS) or conformation of protein based drugs. Starting from the very basics of protein structure, this book explains the best way to achieve this goal using key methods commonly employed in the biopharmaceutical industry. This book will help today’s industrial scientists plan a career in this industry and successfully implement these biophysical methodologies. This updated edition has been fully revised, with new chapters focusing on the use of chromatography and electrophoresis and the biophysical characterization of very large biopharmaceuticals. In addition, best practices of applying statistical analysis to biophysical characterization data is included, along with practical issues associated with the concept of a biopharmaceutical’s developability and the technical decision-making process needed when dealing with biophysical characterization data.

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Detaljer
  • SprogEngelsk
  • Sidetal586
  • Udgivelsesdato18-11-2019
  • ISBN139780444641731
  • Forlag Elsevier Science Ltd
  • FormatPaperback
Størrelse og vægt
  • Vægt940 g
  • coffee cup img
    10 cm
    book img
    19,1 cm
    23,5 cm

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    Instrumentation Drug Data analysis Electrophoresis Risk assessment Data processing Field-flow fractionation Diffusion Conformation Hydrodynamics Chromatography Thermodynamics Protein folding Biopharmaceuticals Fluorescence Aggregation Protein-protein interaction Protein dynamics Biosimilarity Candidate selection Comparability Visual Inspection Reproducibility Dynamic Light Scattering Infrared Size-exclusion chromatography Spectroscopy High-throughput Optical activity Data validation Nanoparticle tracking analysis Biosimilars Conformational changes Biophysical properties Biosimilar Biopharmaceutical Formulation development Biophysical characterization Non-covalent Interactions Monoclonal antibody Therapeutic proteins Record keeping Molecular weight Developability 3-Dimensional structure Advance biophysical tools Analytical target profile (ATP)Target measurement uncertainty (TMU)FUV-CD spectroscopy Biophysical fingerprint Biophysical toolbox Band sedimentation Calibration methods Calibration Standards Circular dichroism (CD)Data collection protocols Common practices Biologics candidate selection Bench-top instrument Biophysical solution properties Differential scanning calorimetry (DSC)Protein formulation Conformational stability Drug variant analysis Dynamic light scattering (DLS)Light scattering (LS)Molecular weight Electric sensing zone method colloidal stability Covalent labeling Coulter Counter Flow microscopy Higher order structure (HOS)Conformation Density gradient sedimentation equilibrium Hydrodynamic volume Glyosylation Drug variant forms Instrument settings Lifecyle approach Log keeping native mass spectrometry Optical cell calibrations physical properties Resonant mass measurements Secondary structure analyses Sedimentation velocity Standard biophysical tools Sedimentation Equilibrium Self-association system suitability Synchrotron radiation circular dichroism (SRCD)Troubleshooting Statistical test of variance Secondary bonds Therapeutic protein stability Temporal structure Totality of the Evidence Small angle x-ray scattering (SAXS)Static light scattering (SLS)Software Visible particles Optical cells You-tube informational videos Light obscuration Reportable value Post-translation modifications (PTMs)Dynamics Websites Sedimentation Coefficient Silent HOS changes Spatial Structure UV-absorbance Subvisible Particles SV-AUC

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