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View Section_8_RG.docx from CHEM 445 at Sonoma State University. CHEMISTRY 445 - Myoglobin and Hemoglobin Watch the lecture videos on myoglobin and hemoglobin. Answers to some of the reading guide
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Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 2nsr: Nitromethane Modified Horse Heart Myoglobin
TY - JOUR. T1 - A harántcsíkolt izom rosttípusainak jellemzése sarcoplasmaticus reticulum (SR) Ca2+-ATP-áz és myoglobin immunhisztokémiával.. AU - Krenács, T.. AU - Molnár, E.. AU - Dobó, E.. AU - Dux, L.. PY - 1989/4/1. Y1 - 1989/4/1. N2 - By the immunohistochemical demonstration of SR calcium ATPase and myoglobin a fibre classification method was developed. Fast fibres showed intense, while slow fibres weak SR calcium ATPase reactivity. Immunohistochemical reaction of myoglobin characterized the oxidative metabolic state of fibres similar to the succinate dehydrogenase (SDH) reaction. By means of SR calcium ATPase and myoglobin immunohistochemistry fibres were classified as slow oxidative (SO), fast oxidative glycolytic (FOG) and fast glycolytic (Fg) groups. The SR calcium ATPase activity of the different fibres varied in the FG greater than FOG greater than SO order, while myoglobin immunoreactivity in the FOG greater than SO greater than FG order. Both proteins studied preserved ...
The range of conformations of macromolecules and the dynamic interconversion between conformations is an important part of the relationship between structure and function. The existence of side-chain conformational substates in two systems is directly demonstrated using traditional X-ray crystallographic refinement methodologies. One system is a mutant met-myoglobin where the phenylalanine at position 46 was replaced by a valine. The other is a low-temperature high-resolution dataset for wild-type CO myoglobin, Multi-conformer refinements, which combine molecular dynamics with X-ray data restraints, are shown to model side-chain substates similar to those identified manually. The two conformations of his64 in the mutant myoglobin and wild-type myoglobin, and three conformations of ser117 in the wild-type myoglobin are found "automatically." Time averaged refinements, which also use a modified molecular dynamics algorithm but is a simulation rather than strictly an optimization, also found ...
Assignments of resonances of the heme and distal amino acid protons in spectra of the CO and O2 complexes of sperm whale myoglobin are reported. These resonances provide information on the conformation of the heme pocket. For oxymyoglobin, the assignments of the heme meso protons disagree with those proposed previously on the basis of partial deuteration experiments. Rapid ring flips about the C beta-C gamma bond are detected for Phe-CD1. Recent claims for two conformational substates of valine-E11 in carbonmonoxymyoglobin (Bradbury, J.H. and Carver, J.A. (1984) Biochemistry 23, 4905-4913) are shown to be in error. The pK of His-97 (FG3) in carbonmonoxymyoglobin has been determined (pK = 5.9). This residue appears to influence many spectroscopic properties of myoglobin. The distal His-E7 in carbonmonoxymyoglobin has pK less than 5.0. Differences in the heme pocket conformation in the CO complexes of myoglobin and leghemoglobin are discussed. These differences may be influential in O2 and CO ...
Myoglobin is a protein that is able to bind oxygen. Myoglobin, which is similar to haemoglobin, is the main oxygen-carrying pigment of muscle tissues.[1] Like haemoglobin, it has a porphyrin ring with an iron atom at its centre. It is in the muscle tissue of most mammals. Seals and other marine mammals have more myoglobin in their muscles than land animals.. In humans, increased level of myoglobin in the serum of the blood can be an indication of myocardial infarction. Other factors for a higher level can be damage to the muscles, epileptic seizures, polytrauma. If the value is much too high, this can lead to kidney failure.. ...
The results of the study by Stewart and colleagues confirm previous findings showing that successful coronary reperfusion leads to an accelerated increase in the levels of plasma markers of myocardial injury in patients treated with thrombolytic therapy for MI (1-3). Changes in the level of myoglobin have been found in almost all previous studies to be useful in detecting coronary reperfusion but may lack specificity because this marker is not cardiac-specific. Rapid increases in CKMB, MB isoforms, and troponin may offer enhanced specificity but may be less sensitive because early changes in levels of these compounds are less marked than those of myoglobin. Differences also exist in the performance of the available assays for these markers. This is important for development of clinical criteria for failure of reperfusion. Nonetheless, available data suggest that using ratios of 60- and 90-minute levels to the initial levels of some of these markers is reasonably accurate for assessing the ...
The physiological role of myoglobin depends on the modulation of heme activity by the protein. The hypothesis that functional properties are governed by conserved residues in the distal pocket has been tested by site-directed mutagenesis of three residues: Leu$\sp{29}$, His$\sp{64}$, and Val$\sp{68}$. To facilitate interpretation of functional data, structures of several mutant myoglobins have been determined by X-ray crystallography. Leu$\sp{29}$ controls the volume of the distal pocket. Since Val$\sp{29}$ does not contact bound ligands, this substitution does not affect ligand affinities significantly. It does permit solvent approach to the heme, thereby increasing the rate of autooxidation. Although the Phe$\sp{29}$ mutant was constructed to reduce the volume of the binding site, dipole-multipole interactions stabilize bound oxygen and reduce the rate of autooxidation substantially. His$\sp{64}$ inhibits oxygen dissociation and autooxidation by hydrogen bonding to the ligand. In conjunction ...
We develop a highly predictive energy function to describe the low temperature crystallographic structure of myoglobin with sub-\AA ngstrom precision. We use the energy function to investigate the way how myoglobin folds.For this we employ the Glauber protocol, with a variable ambient temperature. We first increase the temperature so that the structure unfolds into a random coil. We then lower thetemperature back to its original value, and monitor how the myoglobin folds towards its native state.We find that the folding proceeds by $\alpha$-helix nucleation, and that the ordering of helix formation parallels experimental observations. There is also a molten globule folding intermediate, with a radius of gyration that matches the experimentally measured value. We estimate the relative folding times between a random chain and molten globule, and between molten globule and the native state, and we find that the ratio is consistentwith the experimentally measured values. We also propose a number ...
Mini-myoglobin is a polypeptide fragment (residues 32-139) obtained by limited proteolysis of horse heart apomyoglobin and reconstituted with the natural heme. Its functional properties are very similar to those of native myoglobin and therefore it may represent a model for testing the functional role of the protein fragment encoded by the central exon of myoglobin gene (residues 31-105). Here we have investigated some properties of the nitric oxide derivative of mini-myoglobin in comparison with those of NO-myoglobin, to provide more structural information on the heme pocket residues in addition to that already acquired by electron paramagnetic resonance of the cobalt-substituted mini-myoglobin. At pH 7.0, optical and circular dichroism Soret spectra, as well as electron paramagnetic resonance spectra reveal that the heme orientation in the pocket and the coordination state of the ferrous iron in NO-mini-myoglobin are similar to those of the whole protein. The spectra of the NO-mini-myoglobin ...
Myoglobin has a strong affinity for oxygen when it is in the lungs, and where the pressure is around 100 torr. When it reaches the tissues, where its around 20 torr, the affinity for oxygen is still quite high. This makes myoglobin less efficient of an oxygen transporter than hemoglobin, which loses its affinity for oxygen as the pressure goes down and releases the oxygen into the tissues. Myoglobins strong affinity for oxygen means that it keeps the oxygen binded to itself instead of releasing it into the tissues. ...
Co-Mn-Mg-Al oxides were synthesized using auto-combustion and co-precipitation techniques. Constant ratios were maintained with (Co + Mn + Mg)/Al equal to 3.0, (Co + Mn)/Mg equal to 1.0 and Co/Mn equal to 0.5. The chemical and structural composition, redox properties, oxygen storage capacity and oxygen mobility were analyzed using X-ray fluorescence (XRF), X-ray diffraction (XRD), Raman spectroscopy, scanning electron microscopy (SEM), temperature-programmed reduction of hydrogen (H2-TPR), oxygen storage capacity (OSC), oxygen storage complete capacity (OSCC) and isotopic exchange, respectively. The catalytic behavior of the oxides was evaluated in the total oxidation of a mixture of 250 ppm toluene and 250 ppm 2-propanol. The synthesis methodology affected the crystallite size, redox properties, OSC and oxide oxygen mobility, which determined the catalytic behavior. The co-precipitation method got the most active oxide in the oxidation of the volatile organic compound (VOC) mixture because of the
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Myoglobin, molecular model. Myoglobin is a protein found in muscle tissue, where it binds to and stores oxygen to be used during strenuous exercise. The structure of the globin protein protects the haem (iron) group from being oxidised and destroyed by the oxygen it carries. - Stock Image F006/9417
Myoglobin, molecular model. Myoglobin is a protein found in muscle tissue, where it binds to and stores oxygen to be used during strenuous exercise. The structure of the globin protein protects the haem (iron) group from being oxidised and destroyed by the oxygen it carries. - Stock Image F009/6153
HORI, C.E. et al. The effects of aging temperature and aging time on the oxygen storage capacity of Pt-Rh/CeZrO2 catalysts. Braz. J. Chem. Eng. [online]. 2001, vol.18, n.1, pp.23-33. ISSN 0104-6632. http://dx.doi.org/10.1590/S0104-66322001000100003.. The effects of aging temperature and time on the oxygen storage capacity (OSC) of Pt-Rh-promoted Ce0.75Zr0.25O2 solid solutions were measured and correlated with the BET surface area and noble metal (NM) surface area in the catalysts. The NM surface area is better correlated with OSC than is with the BET surface area. On a practical level, our results demonstrated that, even when operating at 900°C with alternating oxidizing and reducing conditions, these materials deactivate slowly with a near t-1 time dependence. Deactivation rates for these catalysts are dependent on the NM loading with the highest loaded catalysts deactivating roughly half as fast as the lowest loaded catalysts. As the aging temperature is increased from 900°C to 1000°C, the ...
The extent of glycation and conformational changes of horse myoglobin (Mb) upon glycation with N-acetyl-glucosamine (GlcNAc), glucose...
Is there a relation between myocardial salvage and the release patterns of myoglobin and creatine kinase-MB in acute myocardial infarction submitted to thrombolysic ...
The team extracted pure myoglobin from the muscles of mammals - from the land-based cow, to the semi-aquatic otter, all the way up elite divers like the sperm whale.. Led by researcher Scott Mirceta, this painstaking examination traced the changes in myoglobin in deep-diving mammals through 200 million years of evolutionary history.. And it revealed that the best breath-holding divers in the mammal family had evolved a non-stick variety of myoglobin.. The secret, Dr Berenbrink explained, was a subtle but crucial piece of chemical trickery; marine mammal myoglobin is positively charged.. This has important physical consequences. Dr Berenbrink explained: "Like the similar poles of a magnet; the proteins repel one another.". "In this way we think the animals are able to pack really high concentrations of these proteins into their muscles and avoid them sticking together and clogging up the muscles.". Dr Berenbrink said he was excited by the discovery because it helped make sense of the incredible ...
Binding to myoglobin, potentially causing myocardial and skeletal muscle dysfunction.. The most clear-cut mechanism by which CO toxicity occurs is competitive binding to the hemoglobin heme groups. ...The net result is a hemoglobin molecule that is poorly equipped to release oxygen at the tissue level. The decreased oxygen delivery is then sensed centrally, stimulating ventilatory efforts and increasing minute ventilation.... The mean half-life of COHb is 320 minutes (128- 409) in young healthy volunteers on room air. Administration of one hundred percent O2 at one atmosphere reduces the half life to 80.3 minutes, while 100% O2 at three atmospheres will reduce the half life to 23.3 minutes. CO binds to cardiac and skeletal myoglobin as well as hemoglobin (Hb). Cardiac myoglobin binds three times more CO than skeletal myoglobin..... By now, if youre still reading, you may be wondering just what the heck this all means. Well, in a nutshell, it means that if you like training along Dauphin Street ...
TY - JOUR. T1 - Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin. AU - Jue, Thomas. AU - Krishnamoorthi, R.. AU - La Mar, Gerd N.. PY - 1983. Y1 - 1983. UR - http://www.scopus.com/inward/record.url?scp=0000836440&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0000836440&partnerID=8YFLogxK. M3 - Article. AN - SCOPUS:0000836440. VL - 105. SP - 5701. EP - 5703. JO - Journal of the American Chemical Society. JF - Journal of the American Chemical Society. SN - 0002-7863. IS - 17. ER - ...
One major goal of biological physics is the discovery and understanding of the concepts and laws that govern biomolecules, in particular proteins. Since there exist at least 10{sup 5} different proteins, the choice of a suitable prototype is necessary. Myoglobin (Mb) has for many years played the role of such a prototype. It appears to be simple enough so that many of its properties can be understood, yet it is complex enough to display many of the fascinating characteristics of biomolecules. One major achievement in the study of any protein would be the establishment of convincing connections among structure, kinetics, energy landscape, dynamics, and function. We believe that this goal has not yet been reached in any protein, but the present knowledge of Mb gives some hope that the end is near in this case. Here we sketch some of the results that have been obtained in the past fifty or more years in the research on Mb, obtained by an army of investigators. ...
what is the difference in the chemical structures of hemoglobin and myoglobin? Both consist of the same heme complex and a binded protein correct ...
what is the difference in the chemical structures of hemoglobin and myoglobin? Both consist of the same heme complex and a binded protein correct ...
Atassi, M. Z., 1966: Significance of the amino acid composition of proteins I Composition of hemoglobins and myoglobins in relation to their structure, function and evolution
View Notes - Hemoglobin Notes from CH 369 at University of Texas. Myoglobin,anoxygenbindingprotein Hasapolypeptidechainwithanironcontaininghemegroup.
Kohno, Y and Berzofsky, J A., "Genetic control of the immune response to myoglobin. V. Antibody production in vitro is macropahge and t cell-dependent and is under control of two determinant-specific ir genes." (1982). Subject Strain Bibliography 1982. 2543 ...
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I was wondering today whether it would be possible to isolate myoglobin from the blood of a deep diving sea mammal, and cultivate it to inject into humans - ...
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Aerobic life on earth requires efficient management of molecular oxygen (O2). Nature has developed proteins that bind an iron-porphyrin (heme) cofactor as versatile O2 managers. Such hemoproteins, in particular in animals and humans, have been extensively studied, for example, establishing cooperative versus non-cooperative O2 binding to heme iron in tetrameric hemoglobin and monomeric myoglobin, respectively. Today, rising interest in this topic stems from the ongoing discovery of globins with broad functionality in plants and microorganisms.. Three physiologically-relevant heme species can be distinguished in myoglobin and hemoglobin: the ligand-free (deoxy), carbon-monoxide inhibited (carboxy), and O2-bound (oxy) forms. Paramagnetic behaviour has established high-spin Fe(II) in deoxy whereas carboxy is diamagnetic due to low-spin Fe(II). For oxy, a diamagnetic cofactor has been proven. A controversy has remained on the nature of the iron-oxygen bonding in myoglobin and hemoglobin, dating back ...
1MNK: Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin.