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Structural dynamics of myoglobin

Biophysical Chemistry, 2000
Conformational fluctuations have been invoked to explain the observation that the diffusion of small ligands through a protein is a global phenomenon, as suggested (for example) by the oxygen induced fluorescence quenching of buried tryptophans. In enzymes processing large substrates, a channel to the catalytic site is often seen in the crystal ...
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Myoglobin and Hemoglobin

2010
Hemoglobin is the vital protein that conveys oxygen from the lungs to the tissues and facilitates the return of carbon dioxide from the tissues back to the lungs [1]–[6]. Myoglobin accepts and stores the oxygen released by hemoglobin and transports it to the mitochondria. The pathways are shown in Fig. 10.1.
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Haemoglobins and Myoglobins

1975
The solubility of O2 in aqueous media is relatively low; one litre of pure water in equilibrium with air at 20°C and atmospheric pressure dissolves 6.59 cm3 of O293, which corresponds to a 3 × 10−4M solution. This limits the rate of diffusion of O2 from the surface of an organism and also the rate at which O2 can be delivered by a circulatory system ...
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[12] Radioimmunoassay of myoglobin

1982
James T. Willerson   +2 more
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Serum Myoglobin

Archives of Internal Medicine, 1979
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Myoglobine

2008
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Myoglobin

2001
D. Karancsi-Menyhárd   +2 more
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On the Evolution of Myoglobin.

Systematic Zoology, 1979
A. E. Romero-Herrera   +4 more
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