Protein NMR techniques
By: edited by Alexander Shekhtman and David S. Burz
Edition: 3rd ed.
Series: Springer protocols; Methods in molecular biology -- 831; Springer protocols; Methods in molecular biology (Clifton, N.J.) -- v. 831.
Publisher: Humana Press
Published: 2012
Place of publication: New York, N.Y
Language: eng
Number of pages: 518
ISBN-13: 9781617794797; 9781617794803
Subjects: NMR-Spektroskopie; Nuclear magnetic resonance spectroscopy; Magnetische Kernresonanz; Proteins; Analysis; Methode; Magnetic Resonance Spectroscopy; Protein; Proteine
Notes: Includes bibliographical references and index.
Table of contents: title: A novel bacterial expression method with optimized parameters for very high yield production of triple-labeled proteins; title: Isotopic labeling of heterologous proteins in the yeast Pichia pastoris and kluyveromyces lactis; title: Isotope labeling in insect cells; title: Isotope labeling in mammalian cells; title: Cell-free protein production for NMR studies; title: Cell-free membrane protein expression for solid-state NMR; title: Expression and purification of Src-family kinases for solution NMR studies; title: NMR studies of large protein systems; title: Protein dynamics by (15)n nuclear magnetic relaxation; title: Bacterial production and solution NMR studies of a viral membrane ion channel; title: Preparation of the modular multi-domain protein RPA for study by NMR spectroscopy; title: NMR studies of protein-RNA interactions; title: Preparation and optimization of protein-DNA complexes suitable for detailed NMR studies; title: NMR studies of protein-ligand interactions; title: In-cell NMR spectroscopy in escherichia coli; title: Deuterated peptides and proteins: Structure and dynamics studies by MAS solid-state NMR; title: Solid-state NMR spectroscopy of protein complexes; title: Synthesis, purification, and characterization of single helix membrane peptides and proteins for NMR spectroscopy; title: Assignment of backbone resonances in a eukaryotic protein kinase - ERK2 as a representative example; title: Electrostatics of hydrogen exchange for analyzing protein flexibility; title: Fast protein backbone NMR resonance assignment using the batch strategy; title: Comprehensive automation for NMR structure determination of proteins; title: Aria for solution and solid-state NMR; title: Determining protein dynamics from (15)n relaxation data by using dynamics.