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PMR Spectra of Native Proteins
Identification of Resonances and Interpretation of Resonance
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absorption activity adenine adenosine amino acid analysis appears association atom band bases binding Biol bond Brahms buried calculated changes Chem chemical shifts circular dichroism compared complex compounds concentration concluded conformation considered contribution curve denaturation dependence derivatives determined difference discussed effect energy experimental exposed exposure field formation groups higher histidine hydrogen bonding increase indicate interaction involved ionization lysozyme magnetic measurements method methyl modified molecular molecule monomer native nucleic acid nucleosides observed obtained occur optical oxidation pair pentose perturbation phosphate poly positive possible presence properties protein protons purine pyrimidine range reaction reactivity reagent recently reference region relatively residues resonances respect ring rotation shifts shown shows side similar solution solvent specific spectra spectrum stacking strength structure studies suggests Table technique temperature Tinoco titration transition tryptophan tyrosine tyrosyl values