Results 151 to 160 of about 2,013 (172)
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A hemeprotein implicated in oxygen transport into the eye of fish
Comparative Biochemistry and Physiology Part A: Physiology, 1975Abstract 1. 1. Following occlusion of the circulation to the eye of bluefish a ferric hemeprotein (or proteins) appears in the blood plasma of the ophthalmic blood vessels. 2. 2. This protein may play a role in the establishment of elevated oxygen pressures by the choroid rete mirabile. 3. 3.
Jonathan B. Wittenberg +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,
Richard M. Pino +2 more
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Ultrafast absorption and Raman spectroscopy of hemeproteins
Chemical Physics, 1989Abstract The applications of Raman and absorption spectroscopy to understand the photophysics and the dynamics of hemoglobin and myoglobin are discussed. The extension of these techniques to the picosecond and the femtosecond domains is described. Study of hemeprotein reactivity on this ultrafast time scale is advantageous because it simplifies the ...
J.W. Petrich, Jean-Louis Martin
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Hemeproteins: Recent Advances in Quantitative XANES Analysis
AIP Conference Proceedings, 2007Recently, we have shown that multiple scattering (MS) theory, via the MXAN package, is able to reproduce the experimental X‐ray absorption near edge structure (XANES) data of biological samples, in particular hemeproteins, from the rising edge up to ∼150–200 eV above the edge.
A. ARCOVITO +3 more
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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.
Bo Nordén +3 more
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De Novo Designed Hemeproteins As A Redox Catalyst [PDF]
[1990] Proceedings of the Twelfth Annual International Conference of the IEEE Engineering in Medicine and Biology Society, 2005 Synthetic peptides are an attractive candidate for the assembly of biomimetic redox catalysts. We have synthesized series of hemeprotein models (helichrome) which have structured polypeptides as a building unit. Four amphiphilic ahelices were attached to the porphyrin ring covalently so that they interacted with each other to form an a-helical bundle ...
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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.
Sebastian Suarez +5 more
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Syntehsis and structural stability of helichrome as an artificial hemeproteins
Biopolymers, 1990AbstractA detailed procedure is described for the syntehsis of helichrome, which is the first successful example of polypeptide‐based artificial hemeprotein. The segment synthesis‐condensation approach used for the assembly of small proteins has proven to be extremely useful for protein mimetics as well.
Emil Thomas Kaiser, Tomikazu Sasaki
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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.
J. G. Kiselar +5 more
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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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