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Mental and behavioral abnormalities caused by occlusion of the right coronary artery: A case report. [PDF]
Medicine (Baltimore)Xu W, Chen M, Zhang Y, Luo Z.
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Journal of Biomolecular Structure and Dynamics, 2020
Osmolytes are generally well-known for the stabilization of proteins. The stabilizing impact of glucose on the dynamics and structure of myoglobin was probed through molecular simulation‚ docking and spectroscopic procedures.
Rasoul Eslami-Farsani +3 more
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Osmolytes are generally well-known for the stabilization of proteins. The stabilizing impact of glucose on the dynamics and structure of myoglobin was probed through molecular simulation‚ docking and spectroscopic procedures.
Rasoul Eslami-Farsani +3 more
semanticscholar +1 more source
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1978
In previous studies, particularly of primates, a high degree of concordance was obtained between an evolutionary pattern based on comparative anatomy and another based on a reconstruction of the possible pathway of evolution of the myoglobin molecule.
K. A. Joysey +3 more
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In previous studies, particularly of primates, a high degree of concordance was obtained between an evolutionary pattern based on comparative anatomy and another based on a reconstruction of the possible pathway of evolution of the myoglobin molecule.
K. A. Joysey +3 more
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Science, 1992
Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune . This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa
Richard E. Ebel +3 more
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Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune . This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa
Richard E. Ebel +3 more
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Cellular and Molecular Life Sciences CMLS, 1998
The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the ...
Tomohiko Suzuki, K. Imai
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The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the ...
Tomohiko Suzuki, K. Imai
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Acta Physiologica Scandinavica, 1955
Summary.Incorporation of radioiron into myoglobin of the muscles of guinea‐pigs and rats was found to be depressed to a similar extent as into hemoglobin under the effect of exposure to a dose of (500–1,400 r of) roentgen rays, in contrast to hemins, the formation of which is not in close connection with mitotic processes as that of cytochrom b or ...
Åke Åkeson, R. Bonnichsen, G. Hevesy
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Summary.Incorporation of radioiron into myoglobin of the muscles of guinea‐pigs and rats was found to be depressed to a similar extent as into hemoglobin under the effect of exposure to a dose of (500–1,400 r of) roentgen rays, in contrast to hemins, the formation of which is not in close connection with mitotic processes as that of cytochrom b or ...
Åke Åkeson, R. Bonnichsen, G. Hevesy
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The structural dynamics of myoglobin [PDF]
Journal of Structural Biology, 2004 Conformational fluctuations in proteins were initially invoked to explain the observation that diffusion of small ligands through the matrix is a global phenomenon. Small globular proteins contain internal cavities that play a role not only in matrix dynamics but also in controlling function, tracing a pathway for the diffusion of the ligand to and ...
BRUNORI, Maurizio +2 more
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Klinische Wochenschrift, 1966
Wahrend der Schwangerschaft kommt es zu einer Zunahme des Myoglobingehaltes des Myometriums von 22,7 mg-% auf 64,8 mg-% Frischgewicht. Der Anstieg ist im letzten Trimenon am deutlichsten ausgepragt; im 7.–8. Schwangerschaftsmonat bestimmen wir noch einen Myoglobingehalt von 34,8 mg-% im Myometrium des Corpus uteri.
K Huber, F Jaisle
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Wahrend der Schwangerschaft kommt es zu einer Zunahme des Myoglobingehaltes des Myometriums von 22,7 mg-% auf 64,8 mg-% Frischgewicht. Der Anstieg ist im letzten Trimenon am deutlichsten ausgepragt; im 7.–8. Schwangerschaftsmonat bestimmen wir noch einen Myoglobingehalt von 34,8 mg-% im Myometrium des Corpus uteri.
K Huber, F Jaisle
openaire +3 more sources