NMR of Proteins and Nucleic Acids
An introduction to underlying principles and experimental procedures using the newest strategies and techniques for obtaining extensive NMR assignments in biopolymers based on NMR data and the primary structure. Includes an extensive and non-mathematical discussion of 2D NMR and Nulcear Overhauser effects; resonance assignments and structure determination in proteins; and resonance assignments and structure determination in nucleic acids. Enables specialists and non-specialists to evaluate the potentialities and limitations of the method.
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2D NMR A-DNA amide protons amino acid residues antiphase aromatic assignment pathway B-DNA backbone base pairs base protons biopolymers BPTI chemical shifts coherence complete conformation contain corresponding COSY cross peak coupling constants crystal structure diagonal peaks distance geometry duplex example experimental Figure fragments frequency H COSY H NMR H spin H-'H distances H2O solution helices helix heteronuclear hydrogen bonds identified indicated labile protons macromolecules ments methyl molecular molecules multiplet NMR assignments NMR data NMR experiments NMR spectra NOE's NOE’s NOESY spectrum nonlabile protons nucleic acids nucleotides obtained peptide segments phase polynucleotide polypeptide polypeptide chain positions procedures proteins and nucleic random coil relaxation RELAYED-COSY resolution resonance lines ribose secondary structure SECSY sequence sequence-specific resonance assignments sequential assignments sequential connectivities sequential distances side chains solvent spectral regions spectroscopy spin-spin coupling strands structure determination Table tion torsion angles tRNA unique Wagner WŁthrich