Protein NMR techniques

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Bibliographische Detailangaben
Weitere Verfasser: Shekhtman, Alexander (Herausgegeben von), Burz, David S. (Herausgegeben von)
Format: Buch
Sprache:Englisch
Veröffentlicht: New York, N.Y. Humana Press 2012.
Ausgabe:3rd ed.
Schriftenreihe:Springer protocols.
Methods in molecular biology (Clifton, N.J.) ; v. 831.
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Inhaltsangabe:
  • A novel bacterial expression method with optimized parameters for very high yield production of triple-labeled proteins
  • Isotopic labeling of heterologous proteins in the yeast Pichia pastoris and kluyveromyces lactis
  • Isotope labeling in insect cells
  • Isotope labeling in mammalian cells
  • Cell-free protein production for NMR studies
  • Cell-free membrane protein expression for solid-state NMR
  • Expression and purification of Src-family kinases for solution NMR studies
  • NMR studies of large protein systems
  • Protein dynamics by (15)n nuclear magnetic relaxation
  • Bacterial production and solution NMR studies of a viral membrane ion channel
  • Preparation of the modular multi-domain protein RPA for study by NMR spectroscopy
  • NMR studies of protein-RNA interactions
  • Preparation and optimization of protein-DNA complexes suitable for detailed NMR studies
  • NMR studies of protein-ligand interactions
  • In-cell NMR spectroscopy in escherichia coli
  • Deuterated peptides and proteins: Structure and dynamics studies by MAS solid-state NMR
  • Solid-state NMR spectroscopy of protein complexes
  • Synthesis, purification, and characterization of single helix membrane peptides and proteins for NMR spectroscopy
  • Assignment of backbone resonances in a eukaryotic protein kinase - ERK2 as a representative example
  • Electrostatics of hydrogen exchange for analyzing protein flexibility
  • Fast protein backbone NMR resonance assignment using the batch strategy
  • Comprehensive automation for NMR structure determination of proteins
  • Aria for solution and solid-state NMR
  • Determining protein dynamics from (15)n relaxation data by using dynamics.