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Myoglobin features

C20-0072. What features do myoglobin and the cytochromes have in common ... [Pg.1492]

Perhaps the more remarkable features of [myoglobin] are its complexity and its lack of symmetry. The arrangement seems to be almost totally lacking in the kind of regularities which one instinctively anticipates, and it is more complicated than has been predicted by any theory of protein structure. [Pg.116]

The NMR spectra for the different electronic configurations described for myoglobin were also studied for hemoglobin and for the isolated -and -chains (Shulman et al. (99)). The basic spectral features are similar to those of the corresponding myoglobins, but the size of the hyperfine shifts of the heme resonances is quite different. As an illustration the resonances at low fields of deoxymyoglobin and deoxyhemoglobin are compared in Fig. 31. [Pg.108]

Many of these features are evident in the three-dimensional structures of ribonuclease and myoglobin shown in Figure II-3. To understand the common and distinguishing features of the secondary and tertiary structure of various proteins as determined by x-ray crystallographic analysis, the student should study several examples in standard textbooks of biochemistry. [Pg.85]

MCD spectra perhaps provide the best fingerprint for the existence of an FeIV=0 structure. Fig. 8 shows that there is a great similarity between the spectra of horseradish peroxidase compound II, horseradish peroxidase compound X, cytochrome c peroxidase compound I, Pseudomonas aeruginosa peroxidase compound I and ferryl myoglobin at acid pH. Similar features are seen in the spectra of catalase [170] and myoglobin [171] compound II. [Pg.94]


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See also in sourсe #XX -- [ Pg.57 ]




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