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Myoglobin, sperm whale

Mb Sperm whale myoglobin, an oxygen-binding protein 153 amino acid residues. Note that Mb lacks cysteine. [Pg.114]

Both attractive forces and repulsive forces are included in van der Waals interactions. The attractive forces are due primarily to instantaneous dipole-induced dipole interactions that arise because of fluctuations in the electron charge distributions of adjacent nonbonded atoms. Individual van der Waals interactions are weak ones (with stabilization energies of 4.0 to 1.2 kj/mol), but many such interactions occur in a typical protein, and, by sheer force of numbers, they can represent a significant contribution to the stability of a protein. Peter Privalov and George Makhatadze have shown that, for pancreatic ribonuclease A, hen egg white lysozyme, horse heart cytochrome c, and sperm whale myoglobin, van der Waals interactions between tightly packed groups in the interior of the protein are a major contribution to protein stability. [Pg.160]

J.F. Stargardt, F.M. Fiawkridge, and H.L. Landrum, Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode. Anal. Chem. 50, 930-932 (1978). [Pg.597]

Figure 13.5 (a) The structure of sperm whale myoglobin. (From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc.) (b) The oxygen-binding curves of myoglobin and haemoglobin. (Reprinted with permission from Collman et al., 2004. Copyright (2004) American Chemical Society.)... [Pg.217]

Fig. 3. Electron density contours of sperm whale myoglobin at 6 A resolution. Fig. 3. Electron density contours of sperm whale myoglobin at 6 A resolution.
Electron transfer to the protein metal center is monitored spectroscopically. In the case of a heme (FeP), a fast increase in absorbance due to direct reduction of Fe(III)P by Ru(bpy)f is followed by a slower increase in absorbance due to reduction of Fe(III)P by the Ru(II) on the protein surface. Control flash experiments with unmodified proteins show only the fast initial increase in absorbance due to Fe(III)P reduction by Ru(bpy)3. Such control experiments demonstrate for horse heart cytochrome c [21], azurin [28], and sperm whale myoglobin [14] that slow reduction of the heme by the EDTA radical produced in the scavenging step does not occur in competition with intramolecular ET. However, for Candida krusei cytochrome c, the control experiment shows evidence for slow EDTA radical reduction of the heme after initial fast reduetion by Ru(bpy)i+ [19]. [Pg.112]

Fig. 1. Relative positions of the surface histidines (12, 48, 81, and 116) and the heme with its axial histidine in ruthenated sperm whale myoglobin. The edge-edge ET distances are 12.7 (His48), 19.1 (His81), 20.1 (Hisll6), and 22.1 A (Hisl2) [12]... Fig. 1. Relative positions of the surface histidines (12, 48, 81, and 116) and the heme with its axial histidine in ruthenated sperm whale myoglobin. The edge-edge ET distances are 12.7 (His48), 19.1 (His81), 20.1 (Hisll6), and 22.1 A (Hisl2) [12]...
Homologous proteins. Homologous proteins usually crystallize under very different conditions. For example, in our laboratory two homologous proteins crystallize in either 10 mM sodium acetate, pH 3.8, 5 mM DTT, and 50% (v/v) MPD (Weichsel et al, 1996), or 100 mM ammonium sulfate, 30% PEG 6000, and 10 mM DTT (Filson et al, 2003). This technique was first used by Kendrew for solving the structure of sperm whale myoglobin (Kendrew et al., 1954) and has been used in many other structural studies. Currently, this technique is heavily exploited in membrane protein crystallography (Wiener,... [Pg.471]

Chemists have adopted several models for depicting protein structure. These include depiction of all the heavy atoms of the protein (the hydrogen atoms are deleted to keep the model simple enough to be understandable), emphasis on the backbone formed by the a carbon atoms, and ribbon diagrams that illustrate secondary structnral elements. These three models for sperm whale myoglobin are collected in figure 11.3. [Pg.138]

Sites Where CO can be Observed in Pbotoflasb Experiments in Different Species of Sperm Whale Myoglobin (References in tbe Text)... [Pg.14]

FIGURE 2 A one-dimensional NMR spectrum of a globin from a marine blood worm. This protein and sperm whale myoglobin are very close structural analogs, belonging to the same protein structural family and sharing an oxygen-transport function. [Pg.138]

Fig. 39. CD spectrum of Aplysia myoglobin compared to that of sperm whale myoglobin in 0.01 M phosphate buffer, pH 7.4 1071... Fig. 39. CD spectrum of Aplysia myoglobin compared to that of sperm whale myoglobin in 0.01 M phosphate buffer, pH 7.4 1071...
Fig. 1. View of selected parts of the molecular skeleton of Ru(NH3)5 modified(His-48) sperm whale myoglobin (from Ref. S2), modified)... Fig. 1. View of selected parts of the molecular skeleton of Ru(NH3)5 modified(His-48) sperm whale myoglobin (from Ref. S2), modified)...
Kinetics and thermodynamics of long-distance electron transfer in Ru(NH3)5 (His-48) myoglobin (Fig. 1, where selected parts of the molecular skeleton of sperm whale myoglobin with Ru(NH3)5 bonded imidazole of His-48 are illustrated) have also been determined 52). The electron transfer observed is represented by... [Pg.118]


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Myoglobin

Protein sperm whale myoglobin

Ruthenated sperm whale myoglobin

Sperm

Sperm whale

Sperm whale myoglobin, schematic

Whales

Whaling

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