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Oxygen Equilibrium Curve of Concentrated He Robert M Winslow
Structure and Energy Change in Hemoglobin by S Walter Englander
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0.1 M Bis-Tris absorbance absorption acid affinity allosteric amplitude atoms beam Biochem Biochemistry Biol Biophys Bohr effect buffer cell chains Chem component concentration conformational curve deoxy deoxygenated deoxyHb difference spectrum dimers dissociation dynamics effectors electron energy equilibrium EXAFS excitation experimental experiments ferric fluorescence frequency function geminate H NMR HbCO HbO2 heme heme proteins hemoglobin histidine infrared inositol hexaphosphate intensity intermediates kinetics laser ligand ligand binding ligation M. F. Perutz measured method modulated molecular molecule myoglobin nsec observed obtained optical oxidized oxygen oxyhemoglobin parameters phase grating photodissociation photolysis Phys picosecond porphyrin probe proton proton resonances psec pulse quaternary structure Raman rate constants reaction rebinding recombination relaxation residues S-H stretch sample shown in Fig signal solution species spectra spectroscopy stretch band structural changes studies substates subunits T-state temperature tertiary tertiary structure tetramers thermal tion transition unliganded values Volume wavelength XANES