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Showing 1 to 20 of 142 for “"myoglobin"”.
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Motions in myoglobin
"When the structure of myoglobin was first revealed by x-ray crystallography, it was discovered that there was no clear evidence of a pathway for ligands to enter the protein to bind at the heme iron. Motions within the protein are necessary for the protein to function. Pressure release and flash …
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Motions in myoglobin
When the structure of myoglobin was first revealed by x-ray crystallography, it was discovered that there was no clear evidence of a pathway for ligands to enter the protein to bind at the heme iron. Motions within the protein are necessary for the protein to function. Pressure release and flash …
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Species-specific Myoglobin Oxidation
… oxidation product present in meat products. Oxymyoglobin (OxyMb) oxidation is accelerated by HNE adduction. The adduction of HNE to the histidine (His) residues of OxyMb is believed to alter the tertiary structure of OxyMb and make the heme group more vulnerable to oxidation. Previous studies …
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Broken ergodicity in myoglobin
… far-from equilibrium states in sperm whale myoglobin and measured the decays of these states as a function of time under vastly different conditions. Our studies have led us to a completely different mechanism for the longevity of these long-lived states, which is based on the idea that …
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Myoglobin at pH 3: Dynamics of myoglobin with the iron-proximal histidine bond broken
… We measured the rebinding kinetics of CO to myoglobin (Mb) at pH3 in 75% glycerol/water in the Soret from 10K to 300K and 50 ns to 100 s. Below about 200K, the observed nonexponential kinetics is attributed to rebinding from the pocket, process I. The resulting distribution of enthalpic …
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Myoglobin Microsperes and Metalloporphyrin -Peptide Complexes
Addition of disulfide bridges and ionic contacts. We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked tweezers and cyclic peptides. The binding affinities, helicities, and mechanism of binding of linear, tweezers, and cyclic peptides to [Fe …
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Experimental studies of myoglobin recombination kinetics
The kinetics of recombination between the protein myoglobin and oxygen or carbon monoxide have been studied as a function of temperature between 40 K and 350 K. Four distinct kinetic regions have been observed. A transient recorder with a logarithmic time base is described which allows storage of …
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Rate-window methods and myoglobin dynamics
… Properties of the oxygen-storage protein myoglobin (Mb) as a model system for dynamics studies are discussed. Special attention is paid to Mb's physiological role, and the basic quantities that describe the protein's function. Background on ligand binding experiments in Mb is reviewed and …
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Theoretical Circular Dichroism Of Lysozyme, Myoglobin And Collagen And Experimental Circular Dichroism Of Myoglobin And Pea Lectin
… CD observed. Minimization was done on lysozyme, myoglobin and collagen, using the molecular modeling software package, Insight®II to obtain minimum energy structures suitable for CD calculations. Molecular dynamics simulations were performed in water at 300K to create an ensemble of …
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Pressure and temperature dependence of myoglobin kinetics
Recombination kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose …
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Arachidonate oxidation metabolite profiles for myoglobin and a structurally altered form of myoglobin produced in muscle disease or trauma
<p>Myoglobin (Mb) and Myoglobin-H (Mb-H) react with glycerophosphocholine (GPC) lipid in the presence of oxygen. This reaction allows the heme group in the protein the chance to induce peroxidation reactions with the lipid. Several aldehyde products of this type of reaction with arachadonic acid …
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Analysis of Carbon-Monoxide and Dioxygen Binding to Myoglobin
Made available in DSpace on 2015-05-13T15:21:55Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 7606689.PDF: 1889469 bytes, checksum: 3a1efe03abd64a0469a6cb9aeecca8d9 (MD5) Previous issue date: 1975
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Rational design of functional heme copper oxidases in myoglobin
… redesign an existing well-studied heme protein, myoglobin, to mimic the bimetallic, heme-CuB site of HCOs. This is the site where molecular oxygen is converted to water as part of cellular respiration. The conversion of oxygen to water is highly difficult as there are many highly reactive …
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Electron paramagnetic resonance of myoglobin and related ferrous complexes
"Electron paramagnetic resonance spectra of myoglobin (Mb), the 02-storage protein of mammals, are reported for the first time. The EPR signals arise from the biologically active ferrous deoxyMb and photolyzed oxyMb, Mb""(2) complexes. Similar EPR signals were also discovered in photolyzed …
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Solution structure and dynamics of myoglobin and its mutants
… solution structure and function of sperm whale myoglobin. The solution structure of sperm whale myoglobin, with atomic resolution is obtained by using nuclear magnetic resonance spectroscopy (NMR).
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Conformational Relaxation and Kinetic Hole-Burning in Sperm Whale Myoglobin
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1988.
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The effects of extended illumination on CO rebinding to myoglobin
… illumination slows the rate of CO rebinding to myoglobin below 160K where CO is trapped within the protein after photolysis. The process increasing the rebinding barriers is found to be a photon-induced rather than a thermal effect. Rebinding barriers of molecules that are photolyzed do not …
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Conformational relaxation and kinetic hole-burning in sperm whale myoglobin
The charge transfer band near 760nm (band II) in myoglobin (Mb) is sensitive to local heme conformation. In photodissociated MbCO at 5K, the band is red shifted with respect to the deoxy wavelength; the protein structure differs from the equilibrium deoxy structure. After photodissociation the area …
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