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Myoglobin protonation

A sample of the protein, horse heart myoglobin, was dissolved in acidified aqueous acetonitrile (1% formic acid in HjO/CHjCN, 1 1 v/v) at a concentration of 20 pmol/1. This sample was injected into a flow of the same solvent passing at 5 pl/min into the electrospray source to give the mass spectrum of protonated molecular ions [M + nH] shown in (a). The measured ra/z values are given in the table (b), along with the number of protons (charges n) associated with each. The mean relative molecular mass (RMM) is 16,951,09 0.3 Da. Finally, the transformed spectrum, corresponding to the true relative molecular mass, is shown in (c) the observed value is close to that calculated (16,951.4), an error of only 0.002%. [Pg.292]

A typical electrospray spectrum of a high-molecular-weight material, i.e. that of horse heart myoglobin, is shown in Figure 4.11. Each of the ions observed arises from attachment of a different number of protons, and an equivalent number of charges, to the intact molecule. [Pg.165]

Nilsson K et al (2004) The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations quantum refinement. Biophys J 87(5) 3437-3447... [Pg.373]

Table 15.2. Proton hf couplings of aquo-myoglobin (data from Mulks et al.2451 in MHz) ... Table 15.2. Proton hf couplings of aquo-myoglobin (data from Mulks et al.2451 in MHz) ...
Apart from fluorescence, several other methods may be used to obtain time-resolved information. In the case of proteins containing an iron atom, Mossbauer spectroscopy allows the determination, in the iron binding site, of not only root-mean-square shifts of atoms but also the times over which such shifts occur. Detailed investigations of myoglobin have yielded relaxation times on the order of 10 8 Proton NMR spectroscopy can be used to... [Pg.72]

In the case of His/CN systems, structurally pertinent to myoglobin cyanide, peroxidase cyanide, cytochrome c cyanide and the CN derivative of a cytochrome c mutant, where the axial ligand methionine is substituted with alanine (Ala80-cyt c-CN), the simple assignment of the four methyl protons, which is an almost trivial task nowadays, provides direct structural information on the axial ligands, which can be used for structural analysis in solution. The chemical shifts for each... [Pg.158]

An obvious extension to 3D spectroscopy from 2D spectroscopy is the homonu-clear NOESY-NOESY [34]. There are two t variable times and one tj, which after Fourier transform provide three frequency domains. The 3D NOESY-NOESY spectrum of met-myoglobin cyanide, which contains low spin iron(III) in a heme moiety (see Fig. 5.7), has been successfully measured [35]. In Fig. 8.22 a slice of the 3D spectrum is shown at the I2-CH3 height. On the diagonal it shows all the dipolar connectivities between I2-CH3 and other protons off-diagonal... [Pg.295]


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See also in sourсe #XX -- [ Pg.364 ]




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