LEADER 05581nam 2200841Ia 450 001 9910138034503321 005 20200520144314.0 010 $a9781283644037 010 $a1283644037 010 $a9783527644520 010 $a3527644520 010 $a9783527644513 010 $a3527644512 010 $a9783527644506 010 $a3527644504 035 $a(CKB)3280000000000410 035 $a(EBL)871260 035 $a(OCoLC)784885263 035 $a(SSID)ssj0000663725 035 $a(PQKBManifestationID)11441710 035 $a(PQKBTitleCode)TC0000663725 035 $a(PQKBWorkID)10603520 035 $a(PQKB)11436772 035 $a(MiAaPQ)EBC871260 035 $a(Au-PeEL)EBL871260 035 $a(CaPaEBR)ebr10608633 035 $a(CaONFJC)MIL395653 035 $a(PPN)176504176 035 $a(OCoLC)768072879 035 $a(FINmELB)ELB177247 035 $a(Perlego)1014271 035 $a(EXLCZ)993280000000000410 100 $a20111205d2012 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aNMR of biomolecules $etowards mechanistic systems biology /$fedited by Ivano Bertini, Kathleen S. McGreevy, and Giacomo Parigi 205 $a1st ed. 210 $aWeinheim $cWiley-VCH ;$aChichester $cJohn Wiley [distributor]$d2012 215 $a1 online resource (653 p.) 300 $aDescription based upon print version of record. 311 08$a9783527328505 311 08$a3527328505 320 $aIncludes bibliographic references and index. 327 $aNMR of Biomolecules: Towards Mechanistic Systems Biology; Contents; Preface; List of Contributors; List of Abbreviations; Part One: Introduction; 1 NMR and its Place in Mechanistic Systems Biology; 2 Structure of Biomolecules: Fundamentals; 2.1 Structural Features of Proteins; 2.1.1 Introduction: From Primary to Quaternary Structure; 2.1.2 Geometrical and Conformational Properties; 2.1.2.1 Backbone Dihedral Angles; 2.1.2.2 Side-Chain Dihedral Angles; 2.1.3 Secondary Structure Elements in Proteins; 2.1.4 Prediction of Secondary Structure 327 $a2.1.5 Structural Motifs and Structural Domains - Combination of Secondary Structural Elements and Structural Motifs2.1.6 Types of Folds and their Classification; 2.1.6.1 Folds of the ? Class; 2.1.6.2 Folds in the ? Class; 2.1.6.3 Folds in the ?/? Class; 2.1.6.4 Folds in the ? + ? Class; 2.1.7 Tertiary Structure; 2.1.8 Quaternary Structure; 2.2 Nucleic Acids; 2.2.1 Introduction; 2.2.1.1 Conformations; 2.2.2 DNA Structure; 2.2.2.1 B-DNA and Derivatives; 2.2.2.2 A-DNA; 2.2.2.3 Z-DNA; 2.2.2.4 Nonstandard DNA Structures; 2.2.2.4.1 Circular DNA; 2.2.2.4.2 Helical Junction; 2.2.2.4.3 Triple Helix 327 $a2.2.2.4.4 i-Motif2.2.2.4.5 Quadruplex DNA; 2.2.3 RNA Structure; 2.2.3.1 Regular RNA Structure - A-Form Helices; 2.2.3.2 Mismatches, Bulges, and Unusual Base Pairing; 2.2.3.3 Reversal and Alteration of Strand Direction: Commonly Observed Loop and Turn Motifs; 2.2.3.3.1 U-Turn; 2.2.3.3.2 K-Turn; 2.2.3.3.3 C-Loop; 2.2.3.3.4 E-Loop; 2.2.3.4 Tetraloops and Tetraloop-Receptor Contact; 2.2.3.5 Higher-Order RNA Tertiary Structure Elements: Coaxial Stacking Motifs; 2.2.3.6 DNA-RNA Hybrids; 3 What Can be Learned About the Structure and Dynamics of Biomolecules from NMR; 3.1 Proteins Studied by NMR 327 $a3.1.1 Why NMR Structures?3.1.2 NMR Bundle; 3.1.3 Protein Dynamics; 3.1.4 Intermolecular Interactions Involving Proteins; 3.2 Nucleic Acids Studied by NMR; 3.2.1 Structure, Mobility, and Function; Part Two: Role of NMR in the Study of the Structure and Dynamics of Biomolecules; 4 Determination of Protein Structure and Dynamics; 4.1 Determination of Protein Structures; 4.1.1 Resonance Assignment; 4.2 NMR Restraints; 4.2.1 Distance Restraints; 4.2.2 Dihedral Angles; 4.2.3 Residual Dipolar Couplings; 4.3 Structure Calculations; 4.3.1 Traditional; 4.3.2 Automated NOESY Assignment 327 $a4.3.3 Energy Refinement of Protein Structures4.3.4 Chemical Shift-Based Approaches for Protein Structure Determination; 4.4 Validation of Protein Structures; 4.4.1 Experimental Data; 4.4.2 Geometric Quality; 4.5 Protein Dynamics and NMR Observables; 4.5.1 NMR Observables Affected by Dynamics; 4.5.2 NMR Experiments to Measure Dynamics and their Interpretation; 4.6 Protocols; 4.6.1 Sample Labeling; 4.6.2 NMR Assignment; 4.6.3 Manual Collection of Restraints; 4.6.4 Structure Calculations; 4.6.5 Structure Refinement; 4.6.6 Chemical Shift-Based Structure Calculations; 4.6.7 Structure Validation 327 $a4.6.8 Protein Dynamics 330 $aNMR is one of the most powerful methods for imaging of biomolecules. This book is the ultimate NMR guide for researchers in the biomedical community and gives not only background and practical tips but also a forward looking view on the future of NMR in systems biology. 517 3 $aNuclear magnetic resonance of biomolecules 606 $aBiomolecules 606 $aBiological systems 606 $aNuclear magnetic resonance spectroscopy 606 $aSystems biology 615 0$aBiomolecules. 615 0$aBiological systems. 615 0$aNuclear magnetic resonance spectroscopy. 615 0$aSystems biology. 676 $a572 701 $aBertini$b Ivano$09320 701 $aMcGreevy$b Kathleen S$0952567 701 $aParigi$b Giacomo$0952568 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910138034503321 996 $aNMR of biomolecules$92153458 997 $aUNINA