LEADER 01655nam0 22003493i 450 001 SUN0082795 005 20160607104348.612 010 $a01-228-9632-7 010 $a978-01-228-9632-3 100 $a20110322d2003 |0engc50 ba 101 $aeng 102 $aNL 105 $a|||| ||||| 200 1 $aSignal transduction$fBastien D. Gomperts, Ijsbrand M. Kramer, Peter E. R. Tatham 205 $aAmsterdam : Elsevier Academic$b2003 210 $aXIV$d424 p. : ill. ; 25 cm 215 $aL'oggetto digitale è riferito alla 2. edizione, 2009. 620 $dAmsterdam$3SUNL001716 676 $a572.8$cBiologia molecolare. Genetica molecolare. Genetica fisiologica. Acidi nucleici$v22 700 1$aGomperts$b, Bastien D.$3SUNV068533$0512672 701 1$aTatham$b, Peter E. R.$3SUNV068534$0723856 701 1$aKramer$b, Ijsbrand M.$3SUNV068535$0512673 712 $aElsevier$3SUNV000127$4650 790 1$aGomperts, B. D.$zGomperts, Bastien D.$3SUNV103178 790 1$aTatham, P. E. R.$zTatham, Peter E. R.$3SUNV103179 790 1$aKramer, I. M.$zKramer, Ijsbrand M.$3SUNV103180 801 $aIT$bSOL$c20200713$gRICA 856 4 $uhttp://books.google.it/books?id=izTeyIj5mM0C&printsec=frontcover&dq=Signal+transduction&hl=it&ei=P3OITYTwN-qT4Abw7L2nDg&sa=X&oi=book_result&ct=result&resnum=1&ved=0CDAQ6AEwAA#v=onepage&q&f=false 912 $aSUN0082795 950 $aUFFICIO DI BIBLIOTECA DEL DIPARTIMENTO DI SCIENZE E TECNOLOGIE AMBIENTALI BIOLOGICHE E FARMACEUTICHE$d17CONS Kb91 $e17DSV1073 20110322 $sBuono 996 $aSignal transduction$91420614 997 $aUNICAMPANIA LEADER 05258nam 2200661Ia 450 001 9910963811303321 005 20251116191929.0 010 $a1-280-96292-5 010 $a9786610962921 010 $a0-08-047103-X 035 $a(CKB)1000000000364549 035 $a(EBL)287969 035 $a(OCoLC)162129450 035 $a(SSID)ssj0000229617 035 $a(PQKBManifestationID)11195382 035 $a(PQKBTitleCode)TC0000229617 035 $a(PQKBWorkID)10171732 035 $a(PQKB)10713762 035 $a(Au-PeEL)EBL287969 035 $a(CaPaEBR)ebr10167118 035 $a(CaONFJC)MIL96292 035 $a(MiAaPQ)EBC287969 035 $a(PPN)182565394 035 $a(EXLCZ)991000000000364549 100 $a20060623d2007 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aProtein NMR spectroscopy $eprinciples and practice /$feditors, John Cavanagh ... [et al.] 205 $a2nd ed. 210 $aAmsterdam ;$aBoston $cAcademic Press$dc2007 215 $a1 online resource (915 pages) 300 $aDescription based upon print version of record. 311 08$a0-12-164491-X 320 $aIncludes bibliographical references and index. 327 $aFront cover; Title page; Copyright page; Preface; Preface to the First Edition; Acknowledgements; Table of Contents; 1 Classical NMR Spectroscopy; 1.1 Nuclear Magnetism; 1.2 The Bloch Equations; 1.3 The One-Pulse NMR Experiment; 1.4 Linewidth; 1.5 Chemical Shift; 1.6 Scalar Coupling and Limitations of the Bloch Equations; References; 2 Theoretical Description of NMR Spectroscopy; 2.1 Postulates of Quantum Mechanics; 2.2 The Density Matrix; 2.3 Pulses and Rotation Operators; 2.4 Quantum Mechanical NMR Spectroscopy; 2.5 Quantum Mechanics of Multispin Systems; 2.6 Coherence 327 $a2.7 Product Operator Formalism2.8 Averaging of the Spin Hamiltonians and Residual Interactions; References; 3 Experimental Aspects of NMR Spectroscopy; 3.1 NMR Instrumentation; 3.2 Data Acquisition; 3.3 Data Processing; 3.4 Pulse Techniques; 3.5 Spin Decoupling; 3.6 B0 Field Gradients; 3.7 Water Suppression Techniques; 3.8 One-Dimensional 1H NMR Spectroscopy; References; 4 Multidimensional NMR Spectroscopy; 4.1 Two-Dimensional NMR Spectroscopy; 4.2 Coherence Transfer and Mixing; 4.3 Coherence Selection, Phase Cycling, and Field Gradients; 4.4 Resolution and Sensitivity 327 $a4.5 Three- and Four-Dimensional NMR SpectroscopyReferences; 5 Relaxation and Dynamic Processes; 5.1 Introduction and Survey of Theoretical Approaches; 5.2 The Master Equation; 5.3 Spectral Density Functions; 5.4 Relaxation Mechanisms; 5.5 Nuclear Overhauser Effect; 5.6 Chemical Exchange Effects in NMR Spectroscopy; References; 6 Experimental 1H NMR Methods; 6.1 Assessment of the 1D 1H Spectrum; 6.2 COSY-Type Experiments; 6.3 Multiple-Quantum Filtered COSY; 6.4 Multiple-Quantum Spectroscopy; 6.5 TOCSY; 6.6 Cross-Relaxation NMR Experiments; 6.7 1H 3D Experiments; References 327 $a7 Heteronuclear NMR Experiments7.1 Heteronuclear Correlation NMR Spectroscopy; 7.2 Heteronuclear-Edited NMR Spectroscopy; 7.3 13C-13C Correlations: The HCCH-COSY and HCCH-TOCSY Experiments; 7.4 3D Triple-Resonance Experiments; 7.5 Measurement of Scalar Coupling Constants; 7.6 Measurement of Residual Dipolar Coupling Constants; References; 8 Experimental NMR Relaxation Methods; 8.1 Pulse Sequences and Experimental Methods; 8.2 Picosecond-Nanosecond Dynamics; 8.3 Microsecond-Second Dynamics; References; 9 Larger Proteins and Molecular Interactions; 9.1 Larger Proteins 327 $a9.2 Intermolecular Interactions9.3 Methods for Rapid Data Acquisition; References; 10 Sequential Assignment, Structure Determination, and Other Applications; 10.1 Resonance Assignment Strategies; 10.2 Three-Dimensional Solution Structures; 10.3 Conclusion; References; Table of Symbols; List of Figures; List of Tables; Suggested Reading; Biomolecular NMR Spectroscopy; NMR Spectroscopy; Quantum Mechanics; Index; Spin-1/2 Product Operator Equations; Table of Constants 330 $aProtein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments.Important new techniques and applications of NMR spectroscopy have emerged since the f 606 $aProteins$xAnalysis$vLaboratory manuals 606 $aNuclear magnetic resonance spectroscopy$vLaboratory manuals 615 0$aProteins$xAnalysis 615 0$aNuclear magnetic resonance spectroscopy 676 $a572/.636 686 $a35.62$2bcl 686 $a35.71$2bcl 701 $aCavanagh$b John$f1963-$01857008 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910963811303321 996 $aProtein NMR spectroscopy$94457131 997 $aUNINA