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- 000 02962cam a2200397 a 4500
- 008 111121s2012 nyua b 001 0 eng d
- 020 __ |a 9781617794797 : |c CNY1138.00
- 040 __ |a BTCTA |b eng |c BTCTA |d DEBBG |d RML |d SCB |d HNK |d UKMGB |d YDXCP |d BWX |d COO |d DLC
- 050 00 |a QP551 |b .P69728 2012
- 090 __ |a Q51-3/PNM-2/(3)/ED-11
- 099 __ |a CAL 022012075765
- 245 00 |a Protein NMR techniques / |c edited by Alexander Shekhtman and David S. Burz.
- 260 __ |a New York, N.Y. : |b Humana Press, |c c2012.
- 300 __ |a xiv, 518 p. : |b ill. (some col.) ; |c 26 cm.
- 490 0_ |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.
- 700 1_ |a Shekhtman, Alexander.
- 830 _0 |a Methods in molecular biology (Clifton, N.J.) ; |v v. 831.