Results 201 to 210 of about 2,605 (236)
Some of the next articles are maybe not open access.
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins
Inorganic Chemistry, 2020A combination of in silico methods was used to extend the experimental description of the reductive nitrosylation mechanism in ferric hemeproteins with the molecular details of the role of surrounding amino acids. The computational strategy consisted in the estimation of potential energy profiles for the transition process associated with the ...
Nicolás O. Foglia +2 more
openaire +3 more sources
Low temperature optical spectroscopy of low-spin ferric hemeproteins
European Biophysics Journal, 1996We report the Soret absorption spectra (500-350 nm) of the cyanomet derivatives of human hemoglobin and horse myoglobin, in the temperature range 300-20 K and in two different solvents (65% v/v glycerol-water or 65% v/v ethylene glycol-water). In order to obtain information on stereodynamic properties of active site of the two hemeproteins, we perform ...
M, Leone, A, Cupane, L, Cordone
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +1 more source
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
openaire +1 more source
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
openaire +1 more source
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
openaire +1 more source
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
openaire +1 more source

