Sperm whale myoglobin

Additionally, blood pathways are shunted or blocked to certain tissues that are less important to the animal during dives—such as the stomach, while others sustain a steady blood flow- such as the brain. After removal of the protecting groups of 29 , the crude product was purified with reversed-phase high-performance liquid chromatography to yield sperm whale myoglobin- 57—96 -tetracontapeptide These kinetic parameters result in little change in O2 affinity and an increase in isocyanide affinity, relative to the native protein. Myoglobin contains an intracellular heme that facilitates the transport of molecular oxygen by combining with molecular oxygen to form oxymyoglobins. User Account Log in Register Help. The results were analyzed in terms of a simple, single kinetic barrier model and a more detailed three step binding scheme. There will be extra charge for optional service!
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Zeitschrift für Naturforschung C

It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first. Site-directed mutagenesis of a synthetic gene K. Our website will not work properly. For example, the increase in the association rate constant for CO binding at low pH has been suggested to be caused by the protonation of these histidine residues. More from The Telegraph. Pfam protein domain database More
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RCSB PDB - 2W6Y: Crystal structure of Sperm Whale Myoglobin mutant YQR in complex with Xenon

Sixty-five per cent of the heme-containing protein is represented by two of the components, designated as components TV and V, and these have been isolated in quantity for structural study. In contrast, k' for binding to myoglobin is either unchanged RNC or increases CO with increasing glycerol concentration. Select the link destinations: A respectful treatment of one another is important to us. The sperm whale myoglobin produced is stable, easily purified to homogeneity, and indistinguishable from commercially available sperm whale myoglobin by optical and magnetic spectroscopic methods. Select a section on the left to see content.
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AB - Site-directed mutants of sperm whale myoglobin were prepared to probe the functional role of the highly conserved distal pocket valine residue, Val68 E The most dramatic change found at low pH is that His64 swings out of the distal pocket in the MbCO structure at pH 4, opening a direct channel from the solvent to the iron atom. The affinities for all of the ligands were decreased for the Ile68 mutant. About the article Received: You are using a version of browser that may not display all the features of this website.
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