Results 201 to 210 of about 2,618 (230)

Atomic Force Microscopy Studies of Langmuir-Blodgett Films of Cytochrome P450scc: Hemeprotein Aggregation States and Interaction with Lipids

, 1999
Tapping mode atomic force microscopy was applied for a study of the molecular organization and aggregation states of purified bovine adrenocortical cytochrome P450scc present in thin solid films. The films of pure cytochrome P450scc or cytochrome P450scc
O. I. Kiselyova, O. Guryev, A. Krivosheev, S. Usanov, I. Yaminsky   +4 more
semanticscholar   +1 more source

Spin and electron distributions in heme-cyanide models and hemeproteins

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
Proton 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, K.G. Paul, Jan Paul, Michael L. Smith   +3 more
openaire   +3 more sources

Syntehsis and structural stability of helichrome as an artificial hemeproteins

Biopolymers, 1990
AbstractA 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
openaire   +3 more sources

Azanone (HNO) interaction with Hemeproteins and metalloporphyrins

2012
Abstract 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, Fabio Doctorovich, Juan Pellegrino, Damian E. Bikiel, Marcelo A. Martí, Marcelo A. Martí   +5 more
openaire   +2 more sources

Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation.

Developmental and Comparative Immunology, 2021
Zhijie Lu, Mei-Juan Tang, Menglan Zhang, Yanan Li, Fei Shi, F. Zhan, Lijuan Zhao, Jun Li, Li Lin, Zhendong Qin   +9 more
semanticscholar   +1 more source

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 ...
openaire   +1 more source

Peptide scanning in structural -functional mapping of hemeproteins

2006
Peptide 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, G. Hui BonHao, S. A. Moshokoskii, S. A. Kozin, E. F. Kolesanova, Alexander I. Archakov   +5 more
openaire   +2 more sources

Identification and androgen regulation of a 156-kDa hemeprotein in the harderian gland of the Syrian hamster.

General and Comparative Endocrinology, 1996
An abundant cytosolic protein from hamster Harderian glands was partially purified by ultracentrifugation and analyzed on SDS-PAGE. This 156-kDa protein occurs in male but not in female glands.
F. Vilchis, R. Damsky, Y. Heuze, J. Enríquez, B. Chávez   +4 more
semanticscholar   +1 more source

Vibrational Circular Dichroism of Ligand Vibrations in Hemeprotein

1995
The 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.
Y. Matsumoto, H. Sugeta, Yoshimasa Kyogoku, Junji Teraoka, N. Yamamoto   +4 more
openaire   +2 more sources

PI‐INTERACTIONS IN METALLOPORPHYRINS AND HEMEPROTEINS* [PDF]

Annals of the New York Academy of Sciences, 1969
H. Eberspaecher, James O. Alben, W. S. Caughey, W. H. Fuchsman, Sue McCoy   +4 more
openaire   +2 more sources