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Showing 1 to 19 of 19 for “"sperm whale myoglobin"”.
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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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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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The kinetics of protein conformational relaxation in sperm whale myoglobin following a pressure jump
… MPa) dependence of the CO stretching bands in Sperm Whale Myoglobin, Mb, in various solvents has been studied with FTIR spectroscopy. The data are consistent with hierarchically ordered conformational substates, csn' (nth tier), for the protein-ligand-solvent system. The spectra can be resolved …
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Solution structure and dynamics of myoglobin and its mutants
… discusses the 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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Partial structural characterization of the cytoplasmic hemoglobin of Nostoc commune UTEX 584 expressed in Escherichia coli
… quite unlike those of leghemoglobin a and sperm whale myoglobin, which are used as references of comparison. For example, the optical spectral properties of oxycyanoglobin are different from those of leghemoglobin α and sperm whale myoglobin. In addition, the met-form of cyanoglobin has …
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The Influence of Pressure on The Low-Temperature Kinetics of Myoglobin
… of carbon monoxide and dioxygen to horse and sperm whale myoglobin at low temperatures (60 - 160K) was studied using high pressure flash photolysis techniques. By comparing the pressure dependence when the system is first frozen and then pressurized with the pressure dependence when the system …
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Structural heterogeneity and conformational relaxation in heme proteins
… 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 is highly …
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Replacement of Val3 In Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability, Complexes of Sperm Whale Myoglobin G65T With Phenol and Ethylene Glycol, and Structure of A Fragment of Human End-Binding Protein 1 (Eb1)
… inhibitory site.</p> <p>CHAPTER 2: COMPLEXES OF SPERM WHALE MYOGLOBIN (MB) G65T WITH PHENOL AND ETHYLENE GLYCOL.</p> <p>Sperm whale myoglobin (Mb) mutants at position 65 were designed to mimic the heme environment of homologous dehaloperoxidase (DHP). The distance between the distal histidine and …
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Infrared-monitored flash-photolysis of carboxymyoglobin
… A$\sb0$, A$\sb1$, and A$\sb3$ conformations of sperm-whale myoglobin (Mb) at atmospheric pressure and neutral pH are reported. The A$\sb0$, A$\sb1$, and A$\sb3$ rebinding kinetics are shown to be non-exponential and parameterized by activation-enthalpy distributions differing in prefactor …
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Design and Synthesis of Redox or Catalytically Active Artificial Metalloproteins Containing Non-Native Inorganic and Organometallic Complexes
… sites of cytochrome c peroxidase (CcP) and sperm whale myoglobin (Mb) using cysteine residues. The new metalloproteins were characterized by UV-Vis, CD, electrospray mass spectroscopy and cyclic voltammetry. Together with chemical reactivity studies, these results demonstrated that the …
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Control of Ligand Binding to Heme Proteins: The Role 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 time scale of 100 ns to 300 s. Lowering the pH of the …
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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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Control of ligand binding to heme proteins: The role 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 scale of 100 ns to 300 s. Lowering the pH of the …
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Structural and Functional Characterization of Cyanoglobin: A Peripheral Membrane Hemoglobin in Nostoc commune UTEX 584 (Cyanobacteria)
… was more similar to leghemoglobin than to sperm whale myoglobin. The ligand binding behavior of cyanoglobin is explained in terms of a highly reactive, and solvent exposed, heme-iron. The 5' region of glbN interacted with NtcA, the global regulator of nitrogen metabolism in cyanobacteria, …
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Spectroscopic Characterization of H93G Myoglobin Cavity Mutant As A Versatile Protein Scaffold For Modeling Native Heme Iron Coordination Structures and Investigation of the Structure and Mechanism of the Dual-Function Enzyme, Amphitrite Ornata Dehaloperoxidase
<p>His93Gly sperm whale myoglobin (H93G Mb) 'cavity' mutant, having the proximal histidine ligand removed, is a versatile template for establishing the structure of the heme iron coordination unit in proteins. H93G Mb complexes with different exogenous ligands have been successfully prepared as …
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Broken ergodicity in myoglobin
… such transient 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 …
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The role of conformational motions in the control of ligand binding to myoglobin and hemoglobin
Myoglobin and hemoglobin are dioxygen storage and transport proteins. They bind small molecules (ligands) such as dioxygen (02) and carbon monoxide (CO) reversibly. The active site is the heme, a disc shaped molecule which sits in a pocket of the protein (heme pocket). At the center of the heme is …
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Characterization and design of hydrogen bonding interactions in oxygen reduction by engineered myoglobins
… as CuB – was previously structurally modeled in sperm whale myoglobin, by introducing two additional histidine residues, giving a protein called CuBMb. Further structural modeling of this protein to include additional structural features, such as a tyrosine residue, brought about not only partial …
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Engineering heme-copper and multi-copper oxidases for efficient oxygen reduction catalysis
… oxidases. Herein we report a designed oxidase in myoglobin with an O2 reduction rate (52 s−1) comparable to that of a native cytochrome (cyt) cbb3 oxidase (50 s−1) under identical conditions. We achieved this goal by engineering more favorable electrostatic interactions between a functional …