Results 201 to 210 of about 3,386 (219)
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Spin and electron distributions in heme-cyanide models and hemeproteins
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985Proton NMR spectra of low-spin Fe(III) cyanoprotoheme as prosthetic group in a number of proteins are presented. The diagonally positioned 1-, 5- and 3-, 8-methyl groups obey shifts proportional to the Fe(III)/(II) reduction potential Em7, which indicates a pseudo-contact interaction.
J, Paul +3 more
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Permeability of the neonatal rat choriocapillaris to hemeproteins and ferritin
American Journal of Anatomy, 1982AbstractThe permeability of the endothelium of the capillaries of the rat choriocapillaris to circulating macromolecules was examined during the first postnatal week of development using hemeproteins of different molecular dimensions and ferritin. At this stage of development capillaries and photoreceptor cells in the neural retina are not fully formed,
R M, Pino, E, Essner, L C, Pino
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Azanone (HNO) interaction with Hemeproteins and metalloporphyrins
2012Abstract Azanone (HNO), also called nitroxyl, is a highly reactive compound, with interesting yet poorly understood biological properties. Like its closely related sibling NO, its main biological targets are heme proteins, although significant differences in their reactivity and pharmacological effects are observed.
Fabio Doctorovich +4 more
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The Lie-algebraic approach to hemeprotein-ligand dynamics
Chemical Physics Letters, 2003Abstract The Lie-algebraic formalism is applied to the Smoluchowsky’s diffusion equation wherein quantum mechanical ladder operators are used to delineate the Lie-algebra. This approach leads to a simple expression for the survival probability exp( Z 0 ) where Z 0 is the structure constant obtained after solving the equations of motion ...
G. Madhavi Sastry, V. Sabareesh
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Peptide scanning in structural -functional mapping of hemeproteins
2006Peptide scanning (PEPSCAN) is widely used for linear antigenic mapping of proteins, because it reveals almost all possible linear B-epitopes in a protein [1]. To our mind, linear antigenic determinants may have some common structural characteristics, thus allowing antigenic mapping data to be applied in structural studies of proteins.
E. F. Kolesanova +5 more
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Do the hemeproteins behave as a dissipative structure?
International Journal of Quantum Chemistry, 1996Continuing the search for a broader interpretation of hemeprotein behavior, we give preliminary results showing that there are electric and dynamic couplings between the heme group and amino acid residues within the protein matrix. EPR and X-ray absorption spectroscopy studies on azidometmyoglobin show that both magnetic and geometric properties of ...
Bernard Alpert +4 more
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Optical rotatory dispersion of a respiratory hemeprotein of Chrinomus thummi
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968Abstract The spatial structure of an O 2 -binding hemeprotein obtained from Chironomus thummi is compared with that of sperm whale myoglobin by means of rotatory dispersion. The optical rotation at the 233-mμ minimum of the ultraviolet Cotton effect is only 70% of the value obtained for myoglobin.
H, Formanek, J, Engel
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Dynamics of Vibrational Populations in Optically Pumped Hemeproteins
Topical Meeting on Ultrafast Phenomena, 1986Although proteins are disordered materials they can be crystallized and an equilibrium distribution of atomic coordinates can be determined using X-ray diffraction. Thus in contrast to liquids and glasses, the relaxation processes that are induced by the medium can be evaluated in terms of a known equilibrium structure.
E. Henry, W.A. Eaton, R.M. Hochstrasser
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Protein Fluctuations and Hemeprotein Affinity for Ligand
1986Binding processes in hemeproteins involve the iron atom and the protein properties: structural and dynamics. Crystallographic data of Perutz have given an appreciate popularity to a correlation between the displacement of the iron out of the porphyrin plane and the affinity of the hemeprotein for ligand.
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Vibrational Circular Dichroism of Ligand Vibrations in Hemeprotein
1995The distal amino acid residues in myoglobin (Mb) and hemoglobin (Hb) are elaborately designed to control the chemical reactions of ligands to the heme iron. Many techniques have been applied to elucidate the reaction mechanism of ligand binding in heme pockets.
J. Teraoka +4 more
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