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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Online-Zugang:Inhaltsverzeichnis
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245 0 0 |a Protein NMR techniques  |c edited by Alexander Shekhtman and David S. Burz. 
250 |a 3rd ed. 
260 |a New York, N.Y.  |b Humana Press  |c 2012. 
300 |a xiv, 518 p.  |b ill.  |c 26 cm. 
490 1 |a Springer protocols 
490 1 |a Methods in molecular biology  |v 831 
504 |a Includes bibliographical references and index. 
505 0 |a 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. 
650 0 |a Proteins  |x analysis 
650 0 |a Nuclear magnetic resonance spectroscopy 
650 2 |a Magnetic resonance spectroscopy 
650 2 |a Protein 
650 0 7 |a Magnetische Kernresonanz  |2 swd 
650 0 7 |a Methode  |2 swd 
650 0 7 |a NMR-Spektroskopie  |2 swd 
650 0 7 |a proteine  |2 swd 
655 4 |a Aufsatzsammlung 
700 1 |a Shekhtman, Alexander  |4 edt 
700 1 |a Burz, David S.  |4 edt 
830 0 |a Springer protocols. 
830 0 |a Methods in molecular biology (Clifton, N.J.) ;  |v v. 831. 
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