NMR of ProteinsClore, Marius Clore, A. M. Gronenborn This reference represents the most comprehensive and up-to-date collection of biological NMR literature. NMR of Proteins highlights recent advances in the field both with respect to methodology and applications. Four chapters deal with structure determinations of soluble proteins, including approaches for larger proteins, protein modules, and protein-ligand complexes. Other topics include structural studies on membrane proteins, NMR methodology, the investigation of dynamic properties, and protein folding studies. Contributors to this important volume are internationally known experts in their respective fields. |
Contents
Multidimensional NMR studies | 4 |
Methodological advances in protein NMR A Bax | 33 |
Conclusion and outlook | 48 |
Cell adhesion | 54 |
Blood clot homoeostasis | 68 |
NMR structural studies of membrane proteins S J Opella | 159 |
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3D and 4D 3D experiments 3D spectrum 4D NMR amide protons amino acid ascomycin atoms backbone bilayers binding Biochemistry Biol calculated carbon carboxyl Chem chemical shift complex conformation constraints correlation coupling constants cross-peaks cross-relaxation cyclophilin dimensional distance geometry distance restraints domain Driscoll experimental fd coat protein Fesik FKBP folding frequencies helices helix homonuclear hydrogen bonds Ikura interleukin-1ẞ internal motions isotopically labelled larger proteins ligand lysozyme Magn measured membrane proteins methods methyl micelles mobility module molecular dynamics molecules mutant Nilges NMR experiments NMR spectroscopy NMR structures NMR studies NOE interactions NOESY NOESY spectrum nuclear magnetic resonance observed obtained Opella peptide pKa value plastocyanin refinement relaxation rates residues samples secondary structure shown in Figure side-chain simulated annealing SNase solid-state NMR solution structure spectral density stereospecific assignments T₂ T4 lysozyme three-dimensional structure tion torsion angle Wüthrich X-ray structure Zuiderweg