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Showing 1 to 20 of 38 for “"heme proteins"”.
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Ligand Binding by Heme Proteins
Made available in DSpace on 2014-12-14T04:27:34Z (GMT). No. of bitstreams: 1 7606765.pdf: 4038449 bytes, checksum: 62e351e5367503c1cb5b9b986afaa009 (MD5) Previous issue date: 1975
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Optical Activity of Heme Proteins
Made available in DSpace on 2014-12-09T17:36:48Z (GMT). No. of bitstreams: 1 7020980.pdf: 4514168 bytes, checksum: a60db275abc5a904f1eeaaef57d9023a (MD5) Previous issue date: 1970
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Molecular tunneling in heme proteins
Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-27T15:50:04Z No. of bitstreams: 1 1980_reynolds.pdf: 1707453 bytes, checksum: d6a10b7efebee8db106a192f8706c7b8 (MD5)
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Relaxation dynamics in heme proteins
… are protein specific, and which occur in other proteins? How does the environment influence relaxations? (iii) What functional form best describes relaxation functions? (iv) Can we connect the motions to specific structural parts of the protein molecule, and are these motions important for the …
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Relaxation dynamics in heme proteins
A protein molecule possesses many conformational substates that are likely arranged in a hierarchy consisting of a number of tiers. A hierarchical organization of conformational substates is expected to give rise to a multitude of nonequilibrium relaxation phenomena. If the temperature is lowered, …
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Active Site Labeling Studies on Heme Proteins
Made available in DSpace on 2014-12-10T23:01:07Z (GMT). No. of bitstreams: 1 7115008.pdf: 6243868 bytes, checksum: 84013bd36efc9681752aafc04ee3ad77 (MD5) Previous issue date: 1970
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General Features of Ligand Binding to Heme Proteins
The binding of ligands to heme proteins has been studied extensively in the past. A sequential barrier model was postulated. Using flash photolysis, various aspects of the model are studied in this work to give a better understanding of ligand binding. Binding from the pocket, as seen at low …
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Synthetic Iron Porphyrins as Models for Heme Proteins
… been studied as models for the active sites of heme proteins. Spectroscopic studies of (FeTPP)(,2)N('+) (where TPP is the dianion of tetraphenylporphyrin) and (FeTPP)(,2)C indicate that these complexes contain iron(IV). This behavior can be contrasted with the isoelectronic complex …
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Mössbauer investigations of high-spin ferrous heme proteins
"Mössbauer spectroscopy of heme proteins containing iron in the high-spin ferrous state is discussed. Paramagnetic hyperfine interactions, induced by strong applied magnetic fields, result in Mössbauer spectra that contain a wealth of information about the symmetry of the active site iron atomo …
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General features of ligand binding to heme proteins
Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-13T16:03:40Z No. of bitstreams: 1 1983_yue.pdf: 3097209 bytes, checksum: 7a7a4e29cd036d778a7bcba42024cde0 (MD5)
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Structural heterogeneity and conformational relaxation in heme proteins
The influence of cooling rate upon the structural heterogeneity of sperm whale myoglobin solutions at cryogenic temperatures was studied. Sample cooling rates were varied by almost four orders of magnitude. FTIR spectra of the CO stretch frequency region reveal that the population of the A states …
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Multinuclear NMR studies of zeolites and heme-proteins
… systems, zeolites in the solid state and proteins in solution, are investigated, using primarily $\sp{17}$O NMR spectroscopy.
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Conformational relaxation in heme proteins: Ligand rebinding above the glass transition
… the glass-transition temperature of the solvent, heme proteins are frozen into static conformations, and ligand rebinding is well described with a time- and temperature-independent distribution of enthalpic barriers, $g(H)$. This work addresses the relaxation of the enthalpic barriers that sets in …
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pH effects and rebinding pathways in CO adducts of heme proteins
CO-adducts of heme proteins have IR absorption bands over the range 2200-1900 cm$\sp{-1}$. Flash photolysis can break the Fe-C bond, freeing the ligand. Below the glass-transition temperature of the protein-solvent system, $T\sb{g} \approx$ 185K, heme proteins are frozen into static conformations, …
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Conformational relaxation in heme proteins : ligand rebinding above the glass transition
… the glass-transition temperature of the solvent, heme proteins are frozen into static conformations, and ligand rebinding is well described with a time- and temperature-independent distribution of enthalpic barriers, g(H). This work addresses the relaxation of the enthalpic barriers that sets in …
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A migration well model for the binding of ligands to heme proteins
Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-09T14:27:59Z No. of bitstreams: 1 1983_beece.pdf: 3588834 bytes, checksum: 25e21a08d41c0cc111db1e0eaa92b275 (MD5)
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Fast Processes in Heme Proteins: Mechanisms of Electron Transfer and Carbon Monoxide Recombination
An in depth study of carbon monoxide recombination to cytochrome P450$\sb{\rm BM{-}3}$ has shown that this enzyme undergoes a conformational change upon substrate binding. The dynamics of the active site are probed through analysis of the geminate recombination in the presence and absence of …
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Control of Ligand Binding to Heme Proteins: The Role of The Distal Histidine
We have investigated the effect of the distal histidine on the recombination rates of CO and O(,2) to sperm whale myoglobin, separated beta chains of normal human hemoglobin and to the beta chains of hemoglobin Zurich. The recombination was measured using flash photolysis from 300 to 40 K, on a …
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Control of ligand binding to heme proteins: The role of the distal histidine
We have investigated the effect of the distal histidine on the recombination rates of CO and O2 to sperm whale myoglobin, separated beta chains of normal human hemoglobin and to the beta chains of hemoglobin Zurich. The recombination was measured using flash photolysis from 300 to 40 K, on a time …
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Design, Synthesis and Characterization of Heme-proteins: Developing Potential Catalysts for Bio-remediation
… The partial characterization of these proteins revealed the essential structural features of these proteins, and their catalytic activity was demonstrated by the use of peroxidase assays.
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