000			05322cam a2200601Ma 4500
001			ocm70841297
003			OCoLC
005			20141103172220.0
006			m o d
007			cr cnu---uuuuu
008			050418s2005 cauaf ob 001 0 eng d
040			_aYUM _beng _cYUM _dN$T _dYDXCP _dBTCTA _dIDEBK _dE7B _dOCLCQ _dOPELS _dOCLCQ _dOPELS _dOCLCF _dKUK
019			_a171133277 _a173523709 _a178174228 _a648314631
020			_a9780080549477 (electronic bk.)
020			_a0080549470 (electronic bk.)
020			_a0121827992 (electronic bk.)
020			_a9780121827991 (electronic bk.)
035			_a(OCoLC)70841297 _z(OCoLC)171133277 _z(OCoLC)173523709 _z(OCoLC)178174228 _z(OCoLC)648314631
050		4	_aQP601 _b.M49 v.394
072		7	_aSCI _x007000 _2bisacsh
082	0	4	_a572/.7 _222
096			_aQU 25
049			_aTEFA
245	0	0	_aNuclear magnetic resonance of biological macromolecules _h[electronic resource] _nPart C / _cedited by Thomas L. James.
260			_aSan Diego, CA : _bAcademic Press, _cc2005.
300			_a1 online resource (xxxvii, 631 p., [17 leaves of plates]) : _bill. (some col.)
490	1		_aMethods in enzymology ; _vv. 394
550			_aMade available through: Science Direct.
504			_aIncludes bibliographical references and indexes.
505	0		_aIdentification and optimization of protein domains for NMR studies -- In-cell NMR spectroscopy -- Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Shift and Dipolar Homology Database Mining -- Cross-correlated relaxation for structure and dynamics -- Rapid NMR Data Collection -- An Integrated Platform for Automated Analysis of Protein NMR Structures -- Rapid Assessment of Protein Structural Stability and Fold Validation via NMR -- Determination of Protein Backbone Structures from Residual Dipolar Couplings -- Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Consortium -- Protein Structure Estimation From Minimal Restraints Using Rosetta -- Protein Structure Elucidation From Minimal Data: The CLOUDS and ABACUS Approaches -- Elucidation of the Protein Folding Landscape by NMR -- Membrane Protein Preparation for TROSY NMR Screening -- Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP -- NMR Experiments on Aligned Samplet of Membrane Proteins -- NMR techniques used with very large biological macromolecules in solution -- Structure determination of large biological RNAs -- Hydrodynamic Models and Computational Methods for NMR relaxation -- Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High Molecular Weight Systems -- Isotropic Reorientational Eigenmode Dynamics Complements NMR Relaxation Measurements for RNA -- NMR techniques for identifying the interface of a larger protein-protein complex: cross and transferred cross-saturation experiments -- Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy -- Structure determination of protein/RNA complexes by NMR -- Utilization of NMR-derived fragment leads in drug design -- Discovery of Ligands by a Combination of Computational and NMR-based Screening: RNA as an Example Target.
520			_aThe critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences. Nuclear Magnetic Resonance of Biological Macromolecules, Part C is written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules. * One of the most highly respected publications in the field of biochemistry since 1955 * Frequently consulted, and praised by researchers and reviewers alike * Truly an essential publication for anyone in any field of the life sciences.
650		0	_aNuclear magnetic resonance.
650		0	_aMacromolecules.
650	1	2	_aMagnetic Resonance Spectroscopy _xmethods.
650	2	2	_aMacromolecular Substances.
650	2	2	_aPolymers _xchemistry.
650	2	2	_aProteins _xchemistry.
650		7	_aSCIENCE _xLife Sciences _xBiochemistry. _2bisacsh
650		7	_aMacromolecules. _2fast _0(OCoLC)fst01005248
650		7	_aNuclear magnetic resonance. _2fast _0(OCoLC)fst01040325
655		4	_aElectronic books.
700	1		_aJames, Thomas L.
776	0	8	_iPrint version: _tNuclear magnetic resonance of biological macromolecules. Part C. _dSan Diego, CA : Academic Press, c2005 _z0121827992 _z9780121827991 _w(OCoLC)59100279
830		0	_aMethods in enzymology ; _vv. 394.
856	4	0	_3ScienceDirect _uhttp://www.sciencedirect.com/science/book/9780121827991
856	4	0	_3ScienceDirect _uhttp://www.sciencedirect.com/science/bookseries/00766879/394
938			_aYBP Library Services _bYANK _n2614881
938			_aBaker and Taylor _bBTCP _nBK0007476330
938			_aebrary _bEBRY _nebr10188197
938			_aEBSCOhost _bEBSC _n203259
942			_cEB
994			_aC0 _bTEF
999			_c21486 _d21486